Article
A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.
Science (New York, N.Y.) - 24 Aug 1990
Loftus J C, O'Toole T E, Plow E F, Glass A, Frelinger A L, Ginsberg M H
Abstract excerpt
The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant alpha IIb beta 3 integrin (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence of a perturbed interaction with divalent cations. This was found to be caused by a G----T mutat...
Topics
- Amino Acid Sequence
- Animals
- Aspartic Acid
- Base Sequence
- Binding Sites
- Cell Line
- Integrins
- Ligands
- Macromolecular Substances
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes
- Platelet Membrane Glycoproteins
- Polymerase Chain Reaction
- Protein Conformation
- Sequence Homology, Nucleic Acid
- Tyrosine