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...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.