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| | <StructureSection load='5v8z' size='340' side='right'caption='[[5v8z]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5v8z' size='340' side='right'caption='[[5v8z]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[5v8z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.105Å</td></tr> |
| - | <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'>[https://proteopedia.org/fgij/fg.htm?mol=5v8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v8z OCA], [https://pdbe.org/5v8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v8z RCSB], [https://www.ebi.ac.uk/pdbsum/5v8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v8z ProSAT]</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=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> | | </table> |
| | == Function == | | == 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). | + | [https://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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5v8z" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5v8z" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ER-resident protein|ER-resident protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Canlf]] | + | [[Category: Canis lupus familiaris]] |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gehring, K]] | + | [[Category: Gehring K]] |
| - | [[Category: Kozlov, G]] | + | [[Category: Kozlov G]] |
| - | [[Category: Munoz-Escobar, J]] | + | [[Category: Munoz-Escobar J]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein folding]]
| + | |
| Structural highlights
Function
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.
Publication Abstract from PubMed
The lectin chaperones calreticulin (CRT) and calnexin (CNX) contribute to the folding of glycoproteins in the ER by recruiting foldases such as the protein disulfide isomerase ERp57 and the peptidyl prolyl cis-trans isomerase CypB. Recently, CRT was shown to interact with the chaperone ERp29. Here, we show that ERp29 directly binds to the P domain of CNX. Crystal structures of the D domain of ERp29 in complex with the P domains from CRT and calmegin, a tissue-specific CNX homolog, reveal a commonality in the mechanism of binding whereby the tip of the P domain functions as a plurivalent adapter to bind a variety of folding factors. We show that mutation of a single residue, D348 in CNX, abrogates binding to ERp29 as well as ERp57 and CypB. The structural diversity of the accessory factors suggests that these chaperones became specialized for glycoprotein folding through convergent evolution of their P-domain binding sites.
Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones.,Kozlov G, Munoz-Escobar J, Castro K, Gehring K Structure. 2017 Sep 5;25(9):1415-1422.e3. doi: 10.1016/j.str.2017.07.010. PMID:28877505[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kozlov G, Munoz-Escobar J, Castro K, Gehring K. Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones. Structure. 2017 Sep 5;25(9):1415-1422.e3. doi: 10.1016/j.str.2017.07.010. PMID:28877505 doi:http://dx.doi.org/10.1016/j.str.2017.07.010
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