2msb: Difference between revisions

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[[Image:2msb.jpg|left|200px]]
{{Seed}}
[[Image:2msb.png|left|200px]]


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{{STRUCTURE_2msb|  PDB=2msb  |  SCENE=  }}  
{{STRUCTURE_2msb|  PDB=2msb  |  SCENE=  }}  


'''STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE'''
===STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE===




==Overview==
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C-type (Ca(2+)-dependent) animal lectins such as mannose-binding proteins mediate many cell-surface carbohydrate-recognition events. The crystal structure at 1.7 A resolution of the carbohydrate-recognition domain of rat mannose-binding protein complexed with an oligomannose asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds with the carbohydrate ligand. Carbohydrate specificity is determined by a network of coordination and hydrogen bonds that stabilizes the ternary complex of protein, Ca2+ and sugar. Two branches of the oligosaccharide crosslink neighbouring carbohydrate-recognition domains in the crystal, enabling multivalent binding to a single oligosaccharide chain to be visualized directly.
The line below this paragraph, {{ABSTRACT_PUBMED_1436090}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_1436090}}


==About this Structure==
==About this Structure==
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[[Category: Weis, W I.]]
[[Category: Weis, W I.]]
[[Category: Lectin]]
[[Category: Lectin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:34:38 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:06:35 2008''

Revision as of 23:06, 27 July 2008

File:2msb.png

Template:STRUCTURE 2msb

STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE

Template:ABSTRACT PUBMED 1436090

About this Structure

2MSB is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Structure of a C-type mannose-binding protein complexed with an oligosaccharide., Weis WI, Drickamer K, Hendrickson WA, Nature. 1992 Nov 12;360(6400):127-34. PMID:1436090

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