1gya
From Proteopedia
(New page: 200px<br /> <applet load="1gya" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gya" /> '''N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUC...) |
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'''N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2'''<br /> | '''N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The adhesion domain of human CD2 bears a single N-linked carbohydrate. The | + | The adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-(N-acetylglucosamine)2-(mannose)5-8] was solved by nuclear magnetic resonance. The stem and two of three branches of the carbohydrate structure are well defined and the mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather, the carbohydrate stabilizes the protein fold by counterbalancing an unfavorable clustering of five positive charges centered about lysine-61 of CD2. |
==About this Structure== | ==About this Structure== | ||
| - | 1GYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1GYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Choi, J | + | [[Category: Choi, J S.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
| - | [[Category: Wyss, D | + | [[Category: Wyss, D F.]] |
[[Category: cell surface adhesion receptor]] | [[Category: cell surface adhesion receptor]] | ||
[[Category: immunoglobulin superfamily v-set domain]] | [[Category: immunoglobulin superfamily v-set domain]] | ||
[[Category: t lymphocyte adhesion glycoprotein]] | [[Category: t lymphocyte adhesion glycoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:18 2008'' |
Revision as of 10:55, 21 February 2008
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N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2
Overview
The adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-(N-acetylglucosamine)2-(mannose)5-8] was solved by nuclear magnetic resonance. The stem and two of three branches of the carbohydrate structure are well defined and the mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather, the carbohydrate stabilizes the protein fold by counterbalancing an unfavorable clustering of five positive charges centered about lysine-61 of CD2.
About this Structure
1GYA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conformation and function of the N-linked glycan in the adhesion domain of human CD2., Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam AR, Smolyar A, Reinherz EL, Wagner G, Science. 1995 Sep 1;269(5228):1273-8. PMID:7544493
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