1jhn

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{{STRUCTURE_1jhn| PDB=1jhn | SCENE= }}
{{STRUCTURE_1jhn| PDB=1jhn | SCENE= }}
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'''Crystal Structure of the Lumenal Domain of Calnexin'''
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===Crystal Structure of the Lumenal Domain of Calnexin===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11583625 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11583625}}
==About this Structure==
==About this Structure==
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[[Category: Beta sandwich]]
[[Category: Beta sandwich]]
[[Category: Jelly-roll]]
[[Category: Jelly-roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:14:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:15:37 2008''

Revision as of 17:15, 1 July 2008

Image:1jhn.png

Template:STRUCTURE 1jhn

Crystal Structure of the Lumenal Domain of Calnexin

Template:ABSTRACT PUBMED 11583625

About this Structure

1JHN is a Single protein structure of sequence from Canis lupus familiaris. 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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