Mapping functional residues onto integrin crystal structures.
Historical data, available in the literature, concerning the sites responsible for integrin-ligand binding and activation may now be transposed onto recently solved crystal structures of integrin dimers and functional domains. The data were obtained through studies of natural and engineered mutations within integrins, and analyses of the epitopes for function-altering monoclonal antibodies. In the past two years, this combining of structure and function has led to the development of novel hypotheses for the mechanisms of integrin regulation.
Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, United Kingdom. martin.humphries@man.ac.uk
Martin J
MJ
Humphries
Emlyn J H
EJ
Symonds
A Paul
AP
Mould
D001665:Binding Sites; D003461:Crystallography / Q000379:methods*; D018604:Epitope Mapping; D016023:Integrins / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D013329:Structure-Activity Relationship
D016023:Integrins; D008024:Ligands; D021122:Protein Subunits