1CI5

GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)

Summary for 1CI5

• Entry DOI: 10.2210/pdb1ci5/pdb
• NMR Information: BMRB: 4455
• Descriptor: PROTEIN (LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN 3(CD58)) (1 entity in total)
• Functional Keywords: adhesion glycoprotein, immunoglobulin superfamily v-set domain, cell surface receptor, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Lipid-anchor, GPI- anchor: P19256
• Total number of polymer chains: 1
• Total formula weight: 11003.18

Authors

Sun, Z.Y.J.,Dotsch, V.,Kim, M.,Li, J.,Reinherz, E.L.,Wagner, G. (deposition date: 1999-04-07, release date: 1999-06-22, Last modification date: 2023-12-27)

Primary citation

Sun, Z.Y.,Dotsch, V.,Kim, M.,Li, J.,Reinherz, E.L.,Wagner, G.
Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.
EMBO J., 18:2941-2949, 1999

PubMed Abstract: 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.

PubMed: 10357807
DOI: 10.1093/emboj/18.11.2941

Experimental method

SOLUTION NMR