Article
Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations.
Science (New York, N.Y.) - 2 May 2003
Li Renhao, Mitra Neal, Gratkowski Holly, Vilaire Gaston, Litvinov Rustem, Nagasami Chandrasekaran, Weisel John W, Lear James D, DeGrado William F, Bennett Joel S
Abstract excerpt
Transmembrane helices of integrin alpha and beta subunits have been implicated in the regulation of integrin activity. Two mutations, glycine-708 to asparagine-708 (G708N)and methionine-701 to asparagine-701, in the transmembrane helix of the beta3 subunit enabled integrin alphaIIbbeta3 to constitutively bind soluble fibrinogen. Further characterization of the G708N mutant revealed that it induced alphaIIbbeta3...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
