Insights into integrin-ligand binding and activation from the first crystal structure.
Integrin receptors transduce bidirectional signals between extracellular adhesion molecules and intracellular cytoskeletal and signalling molecules. The structural basis of integrin signalling is unknown, but the recent publication of the first crystal structure of the extracellular domain of integrin alphaVbeta3 has provided a number of insights. In this review, previous structure-function analyses of integrins that have employed biochemical and molecular biological approaches are placed in the context of the crystal structure, and novel routes to the development of integrin antagonists are discussed.
Humphries
Martin J
MJ
Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, UK. martin.humphries@man.ac.uk
D001665:Binding Sites / Q000502:physiology; D003461:Crystallography; D006801:Humans; D016023:Integrins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008024:Ligands; D017434:Protein Structure, Tertiary / Q000502:physiology; D012216:Rheumatic Diseases / Q000378:metabolism
D016023:Integrins; D008024:Ligands