3o0v: Difference between revisions
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Revision as of 14:47, 24 April 2013
Crystal structure of the calreticulin lectin domainCrystal structure of the calreticulin lectin domain
Template:ABSTRACT PUBMED 20880849
FunctionFunction
[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).[1] [2]
About this StructureAbout this Structure
3o0v is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Kozlov G, Pocanschi CL, Rosenauer A, Bastos-Aristizabal S, Gorelik A, Williams DB, Gehring K. Structural basis of carbohydrate recognition by calreticulin. J Biol Chem. 2010 Dec 3;285(49):38612-20. Epub 2010 Sep 29. PMID:20880849 doi:10.1074/jbc.M110.168294
- ↑ Kozlov G, Pocanschi CL, Rosenauer A, Bastos-Aristizabal S, Gorelik A, Williams DB, Gehring K. Structural basis of carbohydrate recognition by calreticulin. J Biol Chem. 2010 Dec 3;285(49):38612-20. Epub 2010 Sep 29. PMID:20880849 doi:10.1074/jbc.M110.168294
- ↑ Pocanschi CL, Kozlov G, Brockmeier U, Brockmeier A, Williams DB, Gehring K. Structural and functional relationships between the lectin and arm domains of calreticulin. J Biol Chem. 2011 Jun 7. PMID:21652723 doi:10.1074/jbc.M111.258467