1ci5
From Proteopedia
(New page: 200px<br /> <applet load="1ci5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ci5" /> '''GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN...) |
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'''GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)'''<br /> | '''GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CI5 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:// | + | 1CI5 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=1CI5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: immunoglobulin superfamily v-set domain]] | [[Category: immunoglobulin superfamily v-set domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:35:49 2008'' |
Revision as of 13:35, 15 February 2008
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GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)
Overview
A general strategy is presented here for producing glycan-free forms of, glycoproteins without loss of function by employing apolar-to-polar, mutations of surface residues in functionally irrelevant epitopes. The, success of this structure-based approach was demonstrated through the, expression in Escherichia coli of a soluble 11 kDa adhesion domain, extracted from the heavily glycosylated 55 kDa human CD58 ectodomain. The, solution structure was subsequently determined and binding to its, counter-receptor CD2 studied by NMR. This mutant adhesion domain is, functional as determined by several experimental methods, and the size of, its binding site has been probed by chemical shift perturbations in NMR, titration experiments. The new structural information supports a, 'hand-shake' model of CD2-CD58 interaction involving the GFCC'C" faces of, both CD2 and CD58 adhesion domains. The region responsible for binding, specificity is most likely localized on the C, C' and C" strands and the, C-C' and C'-C" loops on CD58.
About this Structure
1CI5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies., Sun ZY, Dotsch V, Kim M, Li J, Reinherz EL, Wagner G, EMBO J. 1999 Jun 1;18(11):2941-9. PMID:10357807
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