1QA9

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

1QA9 の概要

• エントリーDOI: 10.2210/pdb1qa9/pdb
• 分子名称: HUMAN CD2 PROTEIN, HUMAN CD58 PROTEIN (2 entities in total)
• 機能のキーワード: cell adhesion, ig-like domain, cd2, cd58, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 46041.67

構造登録者

Wang, J.-H.,Smolyar, A.,Tan, K.,Liu, J.-H.,Kim, M.,Sun, Z.J.,Wagner, G.,Reinherz, E.L. (登録日: 1999-04-13, 公開日: 1999-04-29, 最終更新日: 2024-02-14)

主引用文献

Wang, J.H.,Smolyar, A.,Tan, K.,Liu, J.H.,Kim, M.,Sun, Z.Y.,Wagner, G.,Reinherz, E.L.
Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors.
Cell(Cambridge,Mass.), 97:791-803, 1999

PubMed 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.

PubMed: 10380930
DOI: 10.1016/S0092-8674(00)80790-4

実験手法

X-RAY DIFFRACTION (3.2 Å)