The molecular structure of cell adhesion molecules

被引:264
|
作者
Chothia, C [1 ]
Jones, EY [1 ]
机构
[1] OXFORD CTR MOL SCI, MOL BIOPHYS LAB, OXFORD OX1 3QU, ENGLAND
关键词
immunoglobulin classification; binding sites; adhesion complexes;
D O I
10.1146/annurev.biochem.66.1.823
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Considerable advances have been made in our knowledge of the molecular structure of cell adhesion molecules, their binding sites, and adhesion complexes. For the cadherins, protein zero, and CD2, additional experimental data support the insights obtained from structural analysis of their domains and molecular models of their adhesion complexes. For neural cell adhesion molecules, L1, fibronectin, tenascin-C, integrins, and vascular cell adhesion molecules, the molecular structure of domains, and in most cases their binding sites, have been elucidated. The substrate recognition sites in some of these molecules possess rate constants for association and dissociation that permit both rapid cell migration and, through avidity, high-affinity cell-cell interactions.
引用
收藏
页码:823 / 862
页数:40
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