View source for 5v90


==Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin==
<StructureSection load='5v90' size='340' side='right'caption='[[5v90]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5v90]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V90 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.255&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5v90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v90 OCA], [https://pdbe.org/5v90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v90 RCSB], [https://www.ebi.ac.uk/pdbsum/5v90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v90 ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:28877505</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5v90" style="background-color:#fffaf0;"></div>

==See Also==
*[[Calreticulin 3D structures|Calreticulin 3D structures]]
*[[ER-resident protein|ER-resident protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gehring K]]
[[Category: Kozlov G]]
[[Category: Munoz-Escobar J]]