1ccz

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spinqualitylabelsall models 1ccz, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE CD2-BINDING DOMAIN OF CD58 (LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN 3) AT 1.8-A RESOLUTION

Overview

The binding of the cell surface molecule CD58 (formerly lymphocyte, function-associated antigen 3) to its ligand, CD2, significantly increases, the sensitivity of antigen recognition by T cells. This was the first, heterophilic cell adhesion interaction to be discovered and is now an, important paradigm for analyzing the structural basis of cell-cell, recognition. The crystal structure of a CD2-binding chimeric form of CD58, solved to 1.8-A resolution, reveals that the ligand binding domain of CD58, has the expected Ig superfamily V-set topology and shares several of the, hitherto unique structural features of CD2, consistent with previous, speculation that the genes encoding these molecules arose via duplication, of a common precursor. Nevertheless, evidence for considerable divergence, of CD2 and CD58 is also implicit in the structures. Mutations that disrupt, CD2 binding map to the highly acidic surface of the AGFCC'C" beta-sheet of, CD58, which, unexpectedly, lacks marked shape complementarity to the, equivalent, rather more basic CD58-binding face of human CD2. The, specificity of the very weak interactions of proteins mediating cell-cell, recognition may often derive largely from electrostatic complementarity, with shape matching at the protein-protein interface being less exact than, for interactions that combine specificity with high affinity, such as, those involving antibodies.

About this Structure

1CCZ is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution., Ikemizu S, Sparks LM, van der Merwe PA, Harlos K, Stuart DI, Jones EY, Davis SJ, Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4289-94. PMID:10200255

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