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5v8z
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of ERp29 D-domain in complex with the P-domain of calmegin== | |
| - | + | <StructureSection load='5v8z' size='340' side='right' caption='[[5v8z]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5v8z]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Canlf Canlf] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V8Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V8Z FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v90|5v90]]</td></tr> | |
| - | [[Category: | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERP29, C12orf8, ERP28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CLGN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 CANLF])</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=5v8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v8z OCA], [http://pdbe.org/5v8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v8z RCSB], [http://www.ebi.ac.uk/pdbsum/5v8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v8z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ERP29_HUMAN ERP29_HUMAN]] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. [[http://www.uniprot.org/uniprot/CLGN_CANLF CLGN_CANLF]] Functions during spermatogenesis as a chaperone for a range of client proteins that are important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. Required for normal sperm migration from the uterus into the oviduct. Required for normal male fertility. Binds calcium ions (By similarity). | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Canlf]] | ||
| + | [[Category: Human]] | ||
| + | [[Category: Gehring, K]] | ||
| + | [[Category: Kozlov, G]] | ||
| + | [[Category: Munoz-Escobar, J]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Protein folding]] | ||
Revision as of 14:40, 6 November 2017
Crystal structure of ERp29 D-domain in complex with the P-domain of calmegin
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