Article
Mutation of a ligand binding domain of beta 3 integrin. Integral role of oxygenated residues in alpha IIb beta 3 (GPIIb-IIIa) receptor function.
The Journal of biological chemistry - 19 Aug 1994
Bajt M L, Loftus J C
Abstract excerpt
A single amino acid substitution in beta 3 (Asp119 --> Tyr) abrogates the ligand binding function of beta 3 integrins and alters the divalent cation conformation of the platelet integrin alpha IIb beta 3 (GPIIb-IIIa). This aspartic acid residue resides within a conserved cluster of oxygenated res...
Topics
- Amino Acid Sequence
- Animals
- Antibodies, Monoclonal
- Binding Sites
- Binding Sites, Antibody
- CHO Cells
- Conserved Sequence
- Cricetinae
- Fibrinogen
- Integrin beta3
- Integrins
- Mice
- Molecular Sequence Data
- Mutation
- Oxygen
- Platelet Glycoprotein GPIIb-IIIa Complex
- Protein Conformation
- Sequence Homology, Amino Acid