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1r1z
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(New page: 200px<br /><applet load="1r1z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1z, resolution 2.40Å" /> '''The Crystal structur...)
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Revision as of 23:05, 20 November 2007
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The Crystal structure of the Carbohydrate recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals a novel metal binding site and conformational changes associated with calcium ion binding
Overview
p58/ERGIC-53 is a calcium-dependent animal lectin that acts as a cargo, receptor, binding to a set of glycoproteins in the endoplasmic reticulum, (ER) and transporting them to the Golgi complex. It is similar in, structure to calcium-dependent leguminous lectins. We have determined the, structure of the carbohydrate-recognition domain of p58/ERGIC-53 in its, calcium-bound form. The structure reveals localized but large, conformational changes in relation to the previously determined metal, ion-free structure, mapping mostly to the ligand-binding site. It reveals, the presence of two calcium ion-binding sites located 6A apart, one of, which has no equivalent in the plant lectins. The second metal ion-binding, site present in that class of lectins, binding Mn(2+), is absent from, p58/ERGIC-53. The absence of a short loop in the ligand-binding site in, this protein suggests that it has adapted to optimally bind the, high-mannose Man(8)(GlcNAc)(2) glycan common to glycoproteins at the ER, exit stage.
About this Structure
1R1Z is a Single protein structure of sequence from Rattus norvegicus with CA as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding., Velloso LM, Svensson K, Pettersson RF, Lindqvist Y, J Mol Biol. 2003 Dec 12;334(5):845-51. PMID:14643651
Page seeded by OCA on Wed Nov 21 01:12:49 2007
