Year: 2005
Type: review
Abstract: The platelet integrin alpha(IIb)beta(3) is required for platelet aggregation. Like other integrins, alpha(IIb)beta(3) resides on cell surfaces in an equilibrium between inactive and active conformations. Recent experiments suggest that the shift between these conformations involves a global reorganization of the alpha(IIb)beta(3) molecule and disruption of constraints imposed by the heteromeric association of the alpha(IIb) and beta(3) transmembrane and cytoplasmic domains. The biochemical, biophysical, and ultrastructural results that support this conclusion are discussed in this Review.
DOI: 10.1172/jci26989
Author: J. S. Bennett
Institution: University of Pennsylvania
Language: English
Subfield: Immunology and Allergy
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
OpenAlex ID: W2050701385