4ef0
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal Structure of the first catalytic domain of protein disulfide isomerase P5== | |
| - | + | <StructureSection load='4ef0' size='340' side='right' caption='[[4ef0]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | ==Function== | + | <table><tr><td colspan='2'>[[4ef0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EF0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EF0 FirstGlance]. <br> |
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDIA6, ERP5, P5, TXNDC7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ef0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ef0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ef0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ef0 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/PDIA6_HUMAN PDIA6_HUMAN]] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.<ref>PMID:15466936</ref> <ref>PMID:12204115</ref> | [[http://www.uniprot.org/uniprot/PDIA6_HUMAN PDIA6_HUMAN]] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.<ref>PMID:15466936</ref> <ref>PMID:12204115</ref> | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | <references | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
| - | [[Category: Gehring, K | + | [[Category: Gehring, K]] |
| - | [[Category: Kozlov, G | + | [[Category: Kozlov, G]] |
| - | [[Category: Vinaik, R | + | [[Category: Vinaik, R]] |
[[Category: Bip]] | [[Category: Bip]] | ||
[[Category: Disulfide bond isomerization]] | [[Category: Disulfide bond isomerization]] | ||
Revision as of 21:10, 25 December 2014
Crystal Structure of the first catalytic domain of protein disulfide isomerase P5
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