CLNS1A

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Chloride channel, nucleotide-sensitive, 1A
Image:PBB Protein CLNS1A image.jpg
PDB rendering based on 1zyi.
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.

History

Founded 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.

Growth

When 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.

Contents

As 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.

Statistics

As of 11 September, 2007, the "PDB Holdings List" at RCSB reported the following statistics:

Proteins Nucleic Acids Protein/NA complexes Other Total
X-ray diffraction 36223 983 1684 24 38914
NMR 5665 781 134 7 6587
Electron microscopy 105 10 38 0 153
Other 80 4 4 2 90
Total 42073 1778 1860 33 45744

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 format

Through 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 data

The 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.

References

Printed

  • H.M. Berman, K. Henrick, H. Nakamura (2003): Announcing the worldwide Protein Data Bank. Nature Structural Biology 10 (12), p. 980 PMID 14634627.
  • H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne: The Protein Data Bank. Nucleic Acids Research, 28 pp. 235-242 (2000). PMID 10592235
  • Bernstein FC, Koetzle TF, Williams GJ, Meyer Jr EF, Brice MD, Rodgers JR, Kennard O, Shimanouchi T, Tasumi M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J Mol Biol 1977;112:535-542. PMID 875032.
  • E.F. Meyer “The First Years of the Protein Data Bank“, Protein Science 6:1591-1597 (1997)
  • Sussman, JL, Lin, D, Jiang, J, Manning, NO, Prilusky, J, Ritter, O & Abola, EE. Protein data bank (PDB): a database of 3D structural information of biological macromolecules. Acta Cryst 1998; D54:1078-1084. PMID 10089483.

Online

Other external links

Links to enzyme database data

  • [1] The best mapping is provided by Kim Henrick's group at EBI as part of the MSD SIFTS initiative.
  • [2] PDB provide a mapping on their beta site, but it is at the whole PDB level not chain level.
  • [3] Search at BRENDA enzyme database portal.
  • [4] PDBSProtEC:

Molecular graphic visualisation tools

Identifiers
Symbol(s) CLNS1A; CLNS1B; ICln; CLCI
External IDs OMIM: 602158 MGI: 109638 Homologene: 990
RNA expression pattern

Image:PBB GE CLNS1A 209143 s at tn.png

More reference expression data

Orthologs
Human Mouse
Entrez 1207 12729
Ensembl ENSG00000074201 ENSMUSG00000025439
Uniprot P54105 P97506
Refseq NM_001293 (mRNA)
NP_001284 (protein) 		NM_023671 (mRNA)
NP_076160 (protein)
Location Chr 11: 77 - 77.03 Mb Chr 7: 97.57 - 97.59 Mb
Pubmed search [5] [6]

Chloride channel, nucleotide-sensitive, 1A, also known as CLNS1A, is a human gene.[1]



References

Further reading

  • Calinisan V, Gravem D, Chen RP, et al. (2006). "New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium.". Front. Biosci. 11: 1646-66. PMID 16368544.
  • Anguita J, Chalfant ML, Civan MM, Coca-Prados M (1995). "Molecular cloning of the human volume-sensitive chloride conductance regulatory protein, pICln, from ocular ciliary epithelium.". Biochem. Biophys. Res. Commun. 208 (1): 89-95. PMID 7887970.
  • Buyse G, de Greef C, Raeymaekers L, et al. (1996). "The ubiquitously expressed pICln protein forms homomeric complexes in vitro.". Biochem. Biophys. Res. Commun. 218 (3): 822-7. doi:10.1006/bbrc.1996.0146. PMID 8579598.
  • Nagl UO, Erdel M, Schmarda A, et al. (1997). "Chromosomal localization of the genes (CLNS1A and CLNS1B) coding for the swelling-dependent chloride channel ICln.". Genomics 38 (3): 438-41. doi:10.1006/geno.1996.0651. PMID 8975725.
  • Schwartz RS, Rybicki AC, Nagel RL (1997). "Molecular cloning and expression of a chloride channel-associated protein pICln in human young red blood cells: association with actin.". Biochem. J. 327 ( Pt 2): 609-16. PMID 9359436.
  • Bekri S, Adélaïde J, Merscher S, et al. (1998). "Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma.". Cytogenet. Cell Genet. 79 (1-2): 125-31. PMID 9533029.
  • Krapivinsky G, Pu W, Wickman K, et al. (1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology.". J. Biol. Chem. 273 (18): 10811-4. PMID 9556550.
  • Tang CJ, Tang TK (1998). "The 30-kD domain of protein 4.1 mediates its binding to the carboxyl terminus of pICln, a protein involved in cellular volume regulation.". Blood 92 (4): 1442-7. PMID 9694734.
  • Pu WT, Krapivinsky GB, Krapivinsky L, Clapham DE (1999). "pICln inhibits snRNP biogenesis by binding core spliceosomal proteins.". Mol. Cell. Biol. 19 (6): 4113-20. PMID 10330151.
  • Hubert MD, Levitan I, Hoffman MM, et al. (2000). "Modulation of volume regulated anion current by I(Cln).". Biochim. Biophys. Acta 1466 (1-2): 105-14. PMID 10825435.
  • Friesen WJ, Paushkin S, Wyce A, et al. (2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins.". Mol. Cell. Biol. 21 (24): 8289-300. doi:10.1128/MCB.21.24.8289-8300.2001. PMID 11713266.
  • Meister G, Eggert C, Bühler D, et al. (2002). "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln.". Curr. Biol. 11 (24): 1990-4. PMID 11747828.
  • Friesen WJ, Wyce A, Paushkin S, et al. (2002). "A novel WD repeat protein component of the methylosome binds Sm proteins.". J. Biol. Chem. 277 (10): 8243-7. doi:10.1074/jbc.M109984200. PMID 11756452.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Meyer G, Rodighiero S, Guizzardi F, et al. (2004). "Volume-regulated Cl- channels in human pleural mesothelioma cells.". FEBS Lett. 559 (1-3): 45-50. doi:10.1016/S0014-5793(04)00020-1. PMID 14960305.
  • Larkin D, Murphy D, Reilly DF, et al. (2004). "ICln, a novel integrin alphaIIbbeta3-associated protein, functionally regulates platelet activation.". J. Biol. Chem. 279 (26): 27286-93. doi:10.1074/jbc.M402159200. PMID 15075326.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
  • Fürst J, Schedlbauer A, Gandini R, et al. (2005). "ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4.". J. Biol. Chem. 280 (35): 31276-82. doi:10.1074/jbc.M500541200. PMID 15905169.
  • Azzouz TN, Pillai RS, Däpp C, et al. (2005). "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes.". J. Biol. Chem. 280 (41): 34435-40. doi:10.1074/jbc.M505077200. PMID 16087681.
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