3o0v

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<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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [http://www.ebi.ac.uk/pdbsum/3o0v PDBsum]</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=3o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o0v RCSB], [http://www.ebi.ac.uk/pdbsum/3o0v PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/Q3TVD2_MOUSE Q3TVD2_MOUSE]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:20880849</ref> <ref>PMID:21652723</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 11:58, 25 December 2014

Crystal structure of the calreticulin lectin domain

3o0v, resolution 2.30Å

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