Amino Acid Residues in the αIIb Subunit That Are Critical for Ligand Binding to Integrin αIIbβ3 Are Clustered in the β-Propeller Model
Open Access
- 1 November 2001
- journal article
- Published by Elsevier BV
- Vol. 276 (47), 44275-44283
- https://doi.org/10.1074/jbc.m107021200
Abstract
No abstract availableThis publication has 46 references indexed in Scilit:
- Expression and Function of Calcium Binding Domain Chimeras of the Integrins αIIb and α5Published by Elsevier BV ,2000
- Multiple Discontinuous Ligand-mimetic Antibody Binding Sites Define a Ligand Binding Pocket in Integrin αIIbβ3Published by Elsevier BV ,2000
- A Minimized Human Integrin α5β1 That Retains Ligand RecognitionPublished by Elsevier BV ,2000
- Supersites within superfolds. Binding site similarity in the absence of homologyJournal of Molecular Biology, 1998
- Molecular Requirements for Assembly and Function of a Minimized Human Integrin αIIbβ3Online Journal of Public Health Informatics, 1996
- The Amino-terminal One-third of αIIb Defines the Ligand Recognition Specificity of Integrin αIIbβ3Published by Elsevier BV ,1996
- Characterization of the Unique Mechanism Mediating the Shear-dependent Binding of Soluble von Willebrand Factor to PlateletsPublished by Elsevier BV ,1995
- Comparative Protein Modelling by Satisfaction of Spatial RestraintsJournal of Molecular Biology, 1993
- Accurate modeling of protein conformation by automatic segment matchingJournal of Molecular Biology, 1992
- Localization of a site interacting with human platelet receptor on carboxy-terminal segment of human fibrinogen γ chainBiochemical and Biophysical Research Communications, 1982