TLR 2
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| Toll-like receptor 2
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| Available structures: For the file format that describes the 3D structures of molecules found in the Protein Data Bank, see Protein Data Bank (file format).
The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. These data, typically obtained by X-ray crystallography or NMR spectroscopy, are submitted by biologists and biochemists from around the world, are released into the public domain, and can be accessed for free. HistoryFounded in 1971 by Drs. Edgar Meyer and Walter Hamilton Brookhaven National Laboratory, management of the Protein Data Bank was transferred in 1998 to members of the Research Collaboratory for Structural Bioinformatics (RCSB). The Worldwide Protein Data Bank (wwPDB) consists of organizations that act as deposition, data processing and distribution centers for PDB data. The founding members are RCSB PDB (USA), MSD-EBI (Europe) and PDBj (Japan). The BMRB (USA) group joined the wwPDB in 2006. The mission of the wwPDB is to maintain a single Protein Data Bank Archive of macromolecular structural data that is freely and publicly available to the global community. The PDB is a key resource in structural biology and is critical to more recent work in structural genomics. Countless derived databases and projects have been developed to integrate and classify the PDB in terms of protein structure, protein function and protein evolution. GrowthWhen the PDB was originally founded it contained just 7 protein structures. Since then it has undergone an approximate exponential growth in the number of structures, which does not show any sign of falling off. The growth rate of the PDB has been the subject of fairly extensive analysis. ContentsAs of 26 September, 2006, the database contained 39,051 released atomic coordinate entries (or "structures"), 35,767 of that proteins, the rest being nucleic acids, nucleic acid-protein complexes, and a few other molecules. About 5,000 new structures are released each year. Data are stored in the mmCIF format specifically developed for the purpose. Note that the database stores information about the exact location of all atoms in a large biomolecule (although, usually without the hydrogen atoms, as their positions are more of a statistical estimate); if one is only interested in sequence data, i.e. the list of amino acids making up a particular protein or the list of nucleotides making up a particular nucleic acid, the much larger databases from Swiss-Prot and the International Nucleotide Sequence Database Collaboration should be used. StatisticsAs of 11 September, 2007, the "PDB Holdings List" at RCSB reported the following statistics:
Note that theoretical models are no longer accepted in the PDB. 22461 structures in the PDB have a structure factor file. 3138 structures in the PDB have an NMR restraint file. The current breakdown of holdings is updated weekly. File formatThrough the years the PDB file format has undergone many, many changes and revisions. Its original format was dictated by the width of computer punch cards.
This legacy format has caused many problems with the format, and consequently there are 'clean-up' projects; The MMDB uses ASN.1 (and an XML conversion of this format). The wwPDB members RCSB PDB, MSD-EBI, and PDBj are working together to make the data uniform across the archive. Some believe this to be desirable; others argue that, without a universal repository of information (i.e., a common dictionary), it is not possible to draw comparisons. Each structure published in PDB receives a four-character alphanumeric identifier, its PDB ID. This should not be used as an identifier for biomolecules, since often several structures for the same molecule (in different environments or conformations) are contained in PDB with different PDB IDs. If a biologist submits structure data for a protein or nucleic acid, wwPDB staff reviews and annotates the entry. The data are then automatically checked for plausibility. The source code for this validation software has been released for free. The main data base accepts only experimentally derived structures, and not theoretically predicted ones (see protein structure prediction). Various funding agencies and scientific journals now require scientists to submit their structure data to PDB. Viewing the dataThe structural data can be used to visualize the biomolecules with appropriate software, such as VMD, RasMol, PyMOL, Jmol, MDL Chime, QuteMol, web browser VRML plugin or any web-based software designed to visualize and analyse the protein structures such as STING. A recent desktop software addition is Sirius. The RCSB PDB website also contains resources for education, structural genomics, and related software. ReferencesPrinted
Online
Other external links
Links to enzyme database data
Molecular graphic visualisation tools
The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. These data, typically obtained by X-ray crystallography or NMR spectroscopy, are submitted by biologists and biochemists from around the world, are released into the public domain, and can be accessed for free. HistoryFounded in 1971 by Drs. Edgar Meyer and Walter Hamilton Brookhaven National Laboratory, management of the Protein Data Bank was transferred in 1998 to members of the Research Collaboratory for Structural Bioinformatics (RCSB). The Worldwide Protein Data Bank (wwPDB) consists of organizations that act as deposition, data processing and distribution centers for PDB data. The founding members are RCSB PDB (USA), MSD-EBI (Europe) and PDBj (Japan). The BMRB (USA) group joined the wwPDB in 2006. The mission of the wwPDB is to maintain a single Protein Data Bank Archive of macromolecular structural data that is freely and publicly available to the global community. The PDB is a key resource in structural biology and is critical to more recent work in structural genomics. Countless derived databases and projects have been developed to integrate and classify the PDB in terms of protein structure, protein function and protein evolution. GrowthWhen the PDB was originally founded it contained just 7 protein structures. Since then it has undergone an approximate exponential growth in the number of structures, which does not show any sign of falling off. The growth rate of the PDB has been the subject of fairly extensive analysis. ContentsAs of 26 September, 2006, the database contained 39,051 released atomic coordinate entries (or "structures"), 35,767 of that proteins, the rest being nucleic acids, nucleic acid-protein complexes, and a few other molecules. About 5,000 new structures are released each year. Data are stored in the mmCIF format specifically developed for the purpose. Note that the database stores information about the exact location of all atoms in a large biomolecule (although, usually without the hydrogen atoms, as their positions are more of a statistical estimate); if one is only interested in sequence data, i.e. the list of amino acids making up a particular protein or the list of nucleotides making up a particular nucleic acid, the much larger databases from Swiss-Prot and the International Nucleotide Sequence Database Collaboration should be used. StatisticsAs of 11 September, 2007, the "PDB Holdings List" at RCSB reported the following statistics:
Note that theoretical models are no longer accepted in the PDB. 22461 structures in the PDB have a structure factor file. 3138 structures in the PDB have an NMR restraint file. The current breakdown of holdings is updated weekly. File formatThrough the years the PDB file format has undergone many, many changes and revisions. Its original format was dictated by the width of computer punch cards.
This legacy format has caused many problems with the format, and consequently there are 'clean-up' projects; The MMDB uses ASN.1 (and an XML conversion of this format). The wwPDB members RCSB PDB, MSD-EBI, and PDBj are working together to make the data uniform across the archive. Some believe this to be desirable; others argue that, without a universal repository of information (i.e., a common dictionary), it is not possible to draw comparisons. Each structure published in PDB receives a four-character alphanumeric identifier, its PDB ID. This should not be used as an identifier for biomolecules, since often several structures for the same molecule (in different environments or conformations) are contained in PDB with different PDB IDs. If a biologist submits structure data for a protein or nucleic acid, wwPDB staff reviews and annotates the entry. The data are then automatically checked for plausibility. The source code for this validation software has been released for free. The main data base accepts only experimentally derived structures, and not theoretically predicted ones (see protein structure prediction). Various funding agencies and scientific journals now require scientists to submit their structure data to PDB. Viewing the dataThe structural data can be used to visualize the biomolecules with appropriate software, such as VMD, RasMol, PyMOL, Jmol, MDL Chime, QuteMol, web browser VRML plugin or any web-based software designed to visualize and analyse the protein structures such as STING. A recent desktop software addition is Sirius. The RCSB PDB website also contains resources for education, structural genomics, and related software. ReferencesPrinted
Online
Other external links
Links to enzyme database data
Molecular graphic visualisation tools
The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. These data, typically obtained by X-ray crystallography or NMR spectroscopy, are submitted by biologists and biochemists from around the world, are released into the public domain, and can be accessed for free. HistoryFounded in 1971 by Drs. Edgar Meyer and Walter Hamilton Brookhaven National Laboratory, management of the Protein Data Bank was transferred in 1998 to members of the Research Collaboratory for Structural Bioinformatics (RCSB). The Worldwide Protein Data Bank (wwPDB) consists of organizations that act as deposition, data processing and distribution centers for PDB data. The founding members are RCSB PDB (USA), MSD-EBI (Europe) and PDBj (Japan). The BMRB (USA) group joined the wwPDB in 2006. The mission of the wwPDB is to maintain a single Protein Data Bank Archive of macromolecular structural data that is freely and publicly available to the global community. The PDB is a key resource in structural biology and is critical to more recent work in structural genomics. Countless derived databases and projects have been developed to integrate and classify the PDB in terms of protein structure, protein function and protein evolution. GrowthWhen the PDB was originally founded it contained just 7 protein structures. Since then it has undergone an approximate exponential growth in the number of structures, which does not show any sign of falling off. The growth rate of the PDB has been the subject of fairly extensive analysis. ContentsAs of 26 September, 2006, the database contained 39,051 released atomic coordinate entries (or "structures"), 35,767 of that proteins, the rest being nucleic acids, nucleic acid-protein complexes, and a few other molecules. About 5,000 new structures are released each year. Data are stored in the mmCIF format specifically developed for the purpose. Note that the database stores information about the exact location of all atoms in a large biomolecule (although, usually without the hydrogen atoms, as their positions are more of a statistical estimate); if one is only interested in sequence data, i.e. the list of amino acids making up a particular protein or the list of nucleotides making up a particular nucleic acid, the much larger databases from Swiss-Prot and the International Nucleotide Sequence Database Collaboration should be used. StatisticsAs of 11 September, 2007, the "PDB Holdings List" at RCSB reported the following statistics:
Note that theoretical models are no longer accepted in the PDB. 22461 structures in the PDB have a structure factor file. 3138 structures in the PDB have an NMR restraint file. The current breakdown of holdings is updated weekly. File formatThrough the years the PDB file format has undergone many, many changes and revisions. Its original format was dictated by the width of computer punch cards.
This legacy format has caused many problems with the format, and consequently there are 'clean-up' projects; The MMDB uses ASN.1 (and an XML conversion of this format). The wwPDB members RCSB PDB, MSD-EBI, and PDBj are working together to make the data uniform across the archive. Some believe this to be desirable; others argue that, without a universal repository of information (i.e., a common dictionary), it is not possible to draw comparisons. Each structure published in PDB receives a four-character alphanumeric identifier, its PDB ID. This should not be used as an identifier for biomolecules, since often several structures for the same molecule (in different environments or conformations) are contained in PDB with different PDB IDs. If a biologist submits structure data for a protein or nucleic acid, wwPDB staff reviews and annotates the entry. The data are then automatically checked for plausibility. The source code for this validation software has been released for free. The main data base accepts only experimentally derived structures, and not theoretically predicted ones (see protein structure prediction). Various funding agencies and scientific journals now require scientists to submit their structure data to PDB. Viewing the dataThe structural data can be used to visualize the biomolecules with appropriate software, such as VMD, RasMol, PyMOL, Jmol, MDL Chime, QuteMol, web browser VRML plugin or any web-based software designed to visualize and analyse the protein structures such as STING. A recent desktop software addition is Sirius. The RCSB PDB website also contains resources for education, structural genomics, and related software. ReferencesPrinted
Online
Other external links
Links to enzyme database data
Molecular graphic visualisation tools
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| Identifiers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Symbol(s) | TLR2; CD282; TIL4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603028 MGI: 1346060 Homologene: 20695 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| RNA expression pattern | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Human | Mouse | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Entrez | 7097 | 24088 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Ensembl | ENSG00000137462 | ENSMUSG00000027995 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Uniprot | O60603 | Q811T5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refseq | NM_003264 (mRNA) NP_003255 (protein) | NM_011905 (mRNA) NP_036035 (protein) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Location | Chr 4: 154.84 - 154.85 Mb | Chr 3: 83.92 - 83.93 Mb | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Pubmed search | [13] | [14] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
TLR-2 is a biomolecule, which plays a role in the human immune system. TLR-2 is a membrane protein, a receptor, which is expressed on the surface of certain cells and recognizes native or foreign substances, and passes on appropriate signals to the cell and/or the nervous system.
TLR-2 is a member of a large family of homologous Toll-like receptors (TLRs). TLR2 has also been designated as CD282 (cluster of differentiation 282).
Impact
TLR-2 is a membrane receptor found at the surface of immune system cells that recognises many bacterial, fungal, viral and endogenous substances. Phagocytosis of bound materials takes place in endosome/phagosome and a cellular activation, so that the elements of the innate immune system take over such as macrophages, PMN and dendritic cells tasks of the nonspecific immune defense, B1a and form MZB first anti-bodies and uses in the process the specific anti-body formation. Here cytokine is involved e.g. Tumor necrosis factor-alpha (TNF α) and different interleukins (IL-1alpha, IL-1beta, IL-6, IL-8, IL-12). Before TLRs were discovered, some of the materials specified below were grouped under the term so-called "Moduline". By that rather Th1 appropriate cytokine pattern is seen in most experimental models an immune deviation this way, away of the Th2-expression. Conjugates are developed as vaccines or already used without a priori knowledge.
One only 2006 recognized characteristic is the expression of the TLR-2 on the Tregs (special form of the T-cells), which is brought equally to TCR determined proliferation and functional inactivity. Thereby, a disinhibition of the early inflammation phase and the specific anti-body formation is reached. After reduction of the exciter number many exciter-specific Tregs are present, which, now without TLR-2-Signal, become active and the specific like the inflammatory immune reaction to restrain (see also TGF beta, Interleukin 10). Older literature, which attributes a direct immune stimulation effect over TLR-2 to a given substance, must be interpreted under circumstances that the used TLR-2-knockouts has regularly quite few Tregs.
Functionally relevant polymorphism is described, which reduced to a function restriction and thus usually survival rate with infections/sepsis with Gram-positive bacteria leads in particular.
The signal transduction is represented in the article toll-like receptor.
Expression
TLR-2 is expressed on microglia, Schwann cells, monocytes, macrophages, dendritic cells, polymorphonuclear leukocytes, B-cells (B1a, MZB, B2), T-cells including regulatory T cells (CD4, CD25). TLR-2 is likewise in the epithelium of the bronchial tube and the alveoli.
Agonists
| Agonist | Organism |
| Lipoteichoic acid | Gram-positive bacteria |
| Peptidoglycan | Gram-negative and Gram-positive bacteria |
| atypical LPS | Leptospirosis and Porphyromonas gingivalis |
| MALP-2 and MALP-404 (lipoproteins) | Mycoplasma |
| - | Chlamydophila pneumoniae |
| OspA | Borrelia burgdorferi (Lyme disease) |
| Porin | Haemophilus influenzae |
| Antigen mixtures | Propionibacterium acnes |
| LcrV | Yersinia |
| Lipomannan | Mycobacterium: Mycobacterium tuberculosis |
| GPI anchor | Trypanosoma cruzi |
| Lysophosphatidylserine | Schistosoma mansoni |
| Lipophosphoglycan (LPG) | Leishmania major |
| Glycophosphatidylinositol (GPI) | Plasmodium falciparum |
| Zymosan | Saccharomyces cerevisiae |
| - | Malassezia (commensal yeast) |
| Antigen mixtures | Aspergillus fumigatus, Candida albicans |
| hsp60, as peptide transporter and adjuvant for antigen presentation | - |
| - | Herpes simplex virus |
| - | Varicella zoster virus |
| - | Cytomegalovirus (CMV) |
| Hemagglutinin | Measles |
Further reading
- Aderem A, Ulevitch RJ (2000). "Toll-like receptors in the induction of the innate immune response.". Nature 406 (6797): 782-7. doi:10.1038/35021228. PMID 10963608.
- Muzio M, Polentarutti N, Bosisio D, et al. (2001). "Toll-like receptor family and signalling pathway.". Biochem. Soc. Trans. 28 (5): 563-6. PMID 11044375.
- Hallman M, Rämet M, Ezekowitz RA (2002). "Toll-like receptors as sensors of pathogens.". Pediatr. Res. 50 (3): 315-21. PMID 11518816.
- Dziarski R, Gupta D (2001). "Role of MD-2 in TLR2- and TLR4-mediated recognition of Gram-negative and Gram-positive bacteria and activation of chemokine genes.". J. Endotoxin Res. 6 (5): 401-5. PMID 11521063.
- Lien E, Ingalls RR (2002). "Toll-like receptors.". Crit. Care Med. 30 (1 Suppl): S1-11. PMID 11782555.
- Xu D, Komai-Koma M, Liew FY (2005). "Expression and function of Toll-like receptor on T cells.". Cell. Immunol. 233 (2): 85-9. doi:10.1016/j.cellimm.2005.04.019. PMID 15950961.
- Lorenz E (2007). "TLR2 and TLR4 expression during bacterial infections.". Curr. Pharm. Des. 12 (32): 4185-93. PMID 17100621.
Proteins: clusters of differentiation (see also list of human clusters of differentiation) | |
|---|---|
| 1-50 | CD1 (CD1a-c, CD1d) - CD2 - CD3 - CD4 - CD5 - CD8 - CD9 - CD10 - CD11 (CD11a, CD11b, CD11c) - CD13 - CD14 - CD15 - CD16 - CD18 - CD19 - CD20 - CD21 - CD22 - CD23 - CD24 - CD25 - CD26 - CD27 - CD28 - CD29 - CD30 - CD31 - CD32 - CD33 - CD34 - CD35 - CD36 - CD37 -CD38 - CD40 - CD43 - CD44 - CD45 - CD46 - CD49 (CD49a, CD49b, CD49c, CD49d) |
| 51-100 | CD52 - CD53 - CD54 - CD55 - CD56 - CD58 - CD59 - CD61 - CD62 (CD62E, CD62L, CD62P) - CD63 - CD64 - CD66e - CD68 - CD70 - CD71 - CD72 - CD79 - CD80 - CD81 - CD82 - CD83 - CD86 - CD88 - CD89 - CD90 - CD94 - CD95 - CD97 - CD98 |
| 101-350 | CD103 - CD106 - CD114 - CD116 - CD117 - CD118 - CD120 - CD122 - CD130 - CD131 - CD132 - CD133 - CD134 - CD135 - CD137 - CD138 - CD141 - CD142 - CD143 - CD146 - CD147 - CD151 - CD152 - CD153 - CD154 - CD155 - CD162 - CD164 - CD169 - CD184 - CD206 - CD209 - CD257 - CD278 - CD281 - CD282 - CD283 - CD304 |
Transmembrane receptors: immune receptors | |
|---|---|
| Cytokine receptor | Type I: interleukin (IL-2, IL-3) - CSF (Erythropoietin, GM-CSF, G-CSF) - Glycoprotein 130/Oncostatin M - Leukemia inhibitory factor - common subunits (Common gamma chain, CSF2RB) Type II: interleukin (IL22RA2) - interferon (IFNAR, IFNGR) |
| Pattern recognition/Toll-like | TLR 1 - TLR 2 - TLR 3 - TLR 4 - TLR 5 - TLR 6 - TLR 7 - TLR 8 - TLR 9 - TLR 10 |
| Fc receptor | ε (FcεRI, FcεRII) - γ (FcγRI, FcγRII, FcγRIII) - α/μ (FcαRI, Fcα/μR) - Neonatal |
| Lymphocyte homing receptor | CD44 - L-selectin - VLA-4 - LFA-1 |
| other | Antigen receptor (B-cell, T cell) - Complement - Formyl peptide - Immunophilins - Integrin - Killer-cell immunoglobulin-like - Scavenger |
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .
