2msb: Difference between revisions

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New page: left|200px<br /><applet load="2msb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2msb, resolution 1.7Å" /> '''STRUCTURE OF A C-TYPE...
 
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[[Image:2msb.jpg|left|200px]]<br /><applet load="2msb" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2msb.jpg|left|200px]]<br /><applet load="2msb" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2msb, resolution 1.7&Aring;" />
caption="2msb, resolution 1.7&Aring;" />
'''STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE'''<br />
'''STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
2MSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2MSB OCA].  
2MSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MSB OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Drickamer, K.]]
[[Category: Drickamer, K.]]
[[Category: Hendrickson, W.A.]]
[[Category: Hendrickson, W A.]]
[[Category: Weis, W.I.]]
[[Category: Weis, W I.]]
[[Category: CA]]
[[Category: CA]]
[[Category: lectin]]
[[Category: lectin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:45:52 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:54 2008''

Revision as of 19:07, 21 February 2008

File:2msb.jpg


2msb, resolution 1.7Å

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

OverviewOverview

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.

About this StructureAbout this Structure

2MSB is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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