Interleukin 1
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| Interleukin 1, alpha
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| Image:PBB Protein IL1A image.jpg | ||||||||||||||||||||||||||||||||||||||
| PDB rendering based on 2ila. | ||||||||||||||||||||||||||||||||||||||
| 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:
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| Identifiers | ||||||||||||||||||||||||||||||||||||||
| Symbol(s) | IL1A; IL-1A; IL1; IL1-ALPHA; IL1F1 | |||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 147760 MGI: 96542 Homologene: 480 | |||||||||||||||||||||||||||||||||||||
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| RNA expression pattern | ||||||||||||||||||||||||||||||||||||||
| Orthologs | ||||||||||||||||||||||||||||||||||||||
| Human | Mouse | |||||||||||||||||||||||||||||||||||||
| Entrez | 3552 | 16175 | ||||||||||||||||||||||||||||||||||||
| Ensembl | ENSG00000115008 | ENSMUSG00000027399 | ||||||||||||||||||||||||||||||||||||
| Uniprot | P01583 | Q3U0Y6 | ||||||||||||||||||||||||||||||||||||
| Refseq | NM_000575 (mRNA) NP_000566 (protein) | NM_010554 (mRNA) NP_034684 (protein) | ||||||||||||||||||||||||||||||||||||
| Location | Chr 2: 113.25 - 113.26 Mb | Chr 2: 128.99 - 129 Mb | ||||||||||||||||||||||||||||||||||||
| Pubmed search | [5] | [6] | ||||||||||||||||||||||||||||||||||||
| Image:IL1b Crystal Structure.png | |
| Crystal structure of IL-1b | |
| Interleukin 1 beta
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| Identifiers | |
| Symbol | IL1B |
| Alt. Symbols | , IL1F2 |
| Entrez | 3553 |
| HUGO | 5992 |
| OMIM | 147720 |
| PDB | 2MIB |
| RefSeq | NM_000576 |
| UniProt | P01584 |
| Other data | |
| Locus | Chr. 2 q13-q21 |
The Interleukin-1 superfamily
The original members of the IL-1 superfamily are IL-1α, IL-1β, and the IL-1 Receptor antagonist (IL-1RA).
- IL-1α and -β are pro-inflammatory cytokines involved in immune defence against infection.
- The IL-1RA is a molecule that competes for receptor binding with IL-1α and IL-1β, blocking their role in immune activation.
Recent years have seen the addition of other molecules to the IL-1 superfamily including IL-18[1] and six more genes with structural homology to IL-1α, IL-1β or IL-1RA. These latter six members are named IL1F5, IL1F6, IL1F7, IL1F8, IL1F9, and IL1F10. In accord, IL-1α, IL-1β, and IL-1RA have been renamed IL-1F1, IL-1F2, and IL-1F3, respectively.[1][1]
A further putative member of the IL-1 family has been recently described that is called IL-33 or IL-1F11, although this name is not officially accepted in the HGNC gene family nomenclature database.[1]
IL-1α and IL-1β
Both IL-1α and IL-1β are produced by macrophages, monocytes and dendritic cells. They form an important part of the inflammatory response of the body against infection. These cytokines increase the expression of adhesion factors on endothelial cells to enable transmigration of leukocytes, the cells that fight pathogens, to sites of infection and re-set the hypothalamus thermoregulatory center, leading to an increased body temperature which expresses itself as fever. IL-1 is therefore called an endogenous pyrogen. The increased body temperature helps the body's immune system to fight infection. IL-1 is also important in the regulation of hematopoiesis. IL-1β production in peripheral tissue has also been associated with hyperalgesia (increased sensitivity to pain) associated with fever.[1]
For the most part, these two forms of IL-1 bind to the same cellular receptor. This receptor is composed of two related, but non-identical, subunits that transmit intracellular signals via a pathway that is mostly shared with certain other receptors. These include the Toll family of innate immune receptors and the receptor for IL-18.
IL-1α is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. This cytokine is produced by many cell types but is only secreted by monocytes and macrophages. It is produced as a proprotein, which is proteolytically processed by calpain and released in a mechanism that is still not well studied. This gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. It has been suggested that the polymorphism of these genes is associated with rheumatoid arthritis and Alzheimer's disease.
Structure of the IL-1 superfamily
IL-1α and IL-1β are produced as precursor peptides. In other words they are made as a long protein that is then processed to release a shorter, active molecule, which is called the mature protein. Mature IL-1β, for instance, is released from Pro-IL-1β following cleavage by a certain member of the caspase family of proteins, called caspase-1 or the interleukin-1 converting enzyme (ICE). The 3-dimensional structure of the mature forms of each member of the human IL-1 superfamily is composed of 12-14 β-strands producing a barrel-shaped protein.[1]
References
Further reading
- Verweij CL, Bayley JP, Bakker A, Kaijzel EL (2002). "Allele specific regulation of cytokine genes: monoallelic expression of the IL-1A gene.". Adv. Exp. Med. Biol. 495: 129-39. PMID 11774556.
- Griffin WS, Mrak RE (2002). "Interleukin-1 in the genesis and progression of and risk for development of neuronal degeneration in Alzheimer's disease.". J. Leukoc. Biol. 72 (2): 233-8. PMID 12149413.
- Arend WP (2003). "The balance between IL-1 and IL-1Ra in disease.". Cytokine Growth Factor Rev. 13 (4-5): 323-40. PMID 12220547.
- Copeland KF (2006). "Modulation of HIV-1 transcription by cytokines and chemokines.". Mini reviews in medicinal chemistry 5 (12): 1093-101. PMID 16375755.
- Schmidt DR, Kao WJ (2007). "The interrelated role of fibronectin and interleukin-1 in biomaterial-modulated macrophage function.". Biomaterials 28 (3): 371-82. doi:10.1016/j.biomaterials.2006.08.041. PMID 16978691.
- Huynh-Ba G, Lang NP, Tonetti MS, Salvi GE (2007). "The association of the composite IL-1 genotype with periodontitis progression and/or treatment outcomes: a systematic review.". J. Clin. Periodontol. 34 (4): 305-17. doi:10.1111/j.1600-051X.2007.01055.x. PMID 17378887.
External links
Cytokines: interleukins | |
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| IL-1 superfamily | IL-1 (IL-1Ra) - IL-18 - IL-33 |
| IL-6 like/gp130 utilizing | IL-6 - IL-11 - IL-27 - IL-30 - IL-31 |
| IL-10 family | IL-10 - IL-19 - IL-20 - IL-22 - IL-24 - IL-26 |
| Interferon type III | IL-28 - IL-29 |
| Common γ-chain family | IL-2/IL-15 - IL-3 - IL-4 - IL-7 - IL-9 - IL-13 - IL-21 |
| IL-12 family | IL-12 - IL-23 - IL-27 - IL-35 |
| Other | IL-5 - IL-8 - IL-14 - IL-16 - IL-17/IL-25 (A) - IL-32 |
cs:Interleukin-1fr:Interleukine 1 it:Interleuchina 1sr:Интерлеукин 1
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 .
