Article
Two novel mutations in the alpha IIb calcium-binding domains identify hydrophobic regions essential for alpha IIbbeta 3 biogenesis.
Blood - 15 Mar 2003
Mitchell W Beau, Li Ji Hong, Singh Fiza, Michelson Alan D, Bussel James, Coller Barry S, French Deborah L
Abstract excerpt
The recently published crystal structure of the external domains of alphaVbeta3 confirms the prediction that the aminoterminal portion of alphaV, which shares 40% homology with alphaIIb, folds into a beta-propeller structure and that the 4 calcium-binding domains are positioned on the bottom of the propeller. To gain insight into the role of the calcium-binding domains in alphaIIb biogenesis, we characterized...
Topics
- Binding Sites
- Calcium
- Cell Line
- Child
- Gene Expression
- Humans
- Immunoblotting
- Infant
- Isoleucine
- Male
- Models, Molecular
- Mutagenesis
- Mutation
- Platelet Glycoprotein GPIIb-IIIa Complex