1qa9

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spinqualitylabelsall models 1qa9, resolution 3.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3) Counter-Receptors

Overview

Interaction between CD2 and its counterreceptor, CD58 (LFA-3), on opposing, cells optimizes immune recognition, facilitating contacts between helper T, lymphocytes and antigen-presenting cells as well as between cytolytic, effectors and target cells. Here, we report the crystal structure of the, heterophilic adhesion complex between the amino-terminal domains of human, CD2 and CD58. A strikingly asymmetric, orthogonal, face-to-face, interaction involving the major beta sheets of the respective, immunoglobulin-like domains with poor shape complementarity is revealed., In the virtual absence of hydrophobic forces, interdigitating charged, amino acid side chains form hydrogen bonds and salt links at the interface, (approximately 1200 A2), imparting a high degree of specificity albeit, with low affinity (K(D) of approximately microM). These features explain, CD2-CD58 dynamic binding, offering insights into interactions of related, immunoglobulin superfamily receptors.

About this Structure

1QA9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors., Wang JH, Smolyar A, Tan K, Liu JH, Kim M, Sun ZY, Wagner G, Reinherz EL, Cell. 1999 Jun 11;97(6):791-803. PMID:10380930

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