1ci5
From Proteopedia
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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
Page seeded by OCA on Mon Nov 12 16:21:54 2007
