Abstract:
: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.
journal_name
Celljournal_title
Cellauthors
Wang JH,Smolyar A,Tan K,Liu JH,Kim M,Sun ZY,Wagner G,Reinherz ELdoi
10.1016/s0092-8674(00)80790-4subject
Has Abstractpub_date
1999-06-11 00:00:00pages
791-803issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80790-4journal_volume
97pub_type
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