1jhn
From Proteopedia
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| - | [[Image:1jhn.gif|left|200px]] | + | [[Image:1jhn.gif|left|200px]] |
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| - | '''Crystal Structure of the Lumenal Domain of Calnexin''' | + | {{Structure |
| + | |PDB= 1jhn |SIZE=350|CAPTION= <scene name='initialview01'>1jhn</scene>, resolution 2.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of the Lumenal Domain of Calnexin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JHN is a [ | + | 1JHN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11583625 11583625] |
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: jelly-roll]] | [[Category: jelly-roll]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:03:30 2008'' |
Revision as of 10:03, 20 March 2008
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| , resolution 2.9Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:03:30 2008
