1jhn
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(New page: 200px<br /><applet load="1jhn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jhn, resolution 2.9Å" /> '''Crystal Structure of ...)
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Revision as of 16:08, 20 November 2007
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Crystal Structure of the Lumenal Domain of Calnexin
Overview
The three-dimensional structure of the lumenal domain of the lectin-like, chaperone calnexin determined to 2.9 A resolution reveals an extended 140, A arm inserted into a beta sandwich structure characteristic of legume, lectins. The arm is composed of tandem repeats of two proline-rich, sequence motifs which interact with one another in a head-to-tail fashion., Identification of the ligand binding site establishes calnexin as a, monovalent lectin, providing insight into the mechanism by which the, calnexin family of chaperones interacts with monoglucosylated, glycoproteins.
About this Structure
1JHN is a Single protein structure of sequence from Canis lupus familiaris with CA as ligand. Full crystallographic information is available from OCA.
Reference
The Structure of calnexin, an ER chaperone involved in quality control of protein folding., Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M, Mol Cell. 2001 Sep;8(3):633-44. PMID:11583625
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