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Annu Rev Cell Dev Biol. 2005;21:381-410.

Integrin structure, allostery, and bidirectional signaling.

Author information

1
Structural Biology Program, Leukocyte Biology and Inflammation Program, Nephrology Division, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachussetts 02129, USA. arnaout@receptor.mgh.harvard.edu

Abstract

Alphabeta heterodimeric integrins mediate dynamic adhesive cell-cell and cell-extracellular matrix (ECM) interactions in metazoa that are critical in growth and development, hemostasis, and host defense. A central feature of these receptors is their capacity to change rapidly and reversibly their adhesive functions by modulating their ligand-binding affinity. This is normally achieved through interactions of the short cytoplasmic integrin tails with intracellular proteins, which trigger restructuring of the ligand-binding site through long-range conformational changes in the ectodomain. Ligand binding in turn elicits conformational changes that are transmitted back to the cell to regulate diverse responses. The publication of the integrin alphaVbeta3 crystal structure has provided the context for interpreting decades-old biochemical studies. Newer NMR, crystallographic, and EM data, reviewed here, are providing a better picture of the dynamic integrin structure and the allosteric changes that guide its diverse functions.

[Indexed for MEDLINE]

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