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1gya
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(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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Revision as of 15:03, 12 November 2007
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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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