Biophysical analysis of kindlin-3 reveals an elongated conformation and maps integrin binding to the membrane-distal β-subunit NPXY motif

Abstract

Background: Kindlins are essential co-activators of integrins. Results: Kindlin-3 has an elongated structure and forms a ternary complex with the Talin head and integrin β-tails. The Kindlin-3-tail interface involves a membrane-distal NPXY motif on the tail. Conclusion: New information about the conformation and interactions of Kindlin-3 has been obtained. Significance: The solution structure and protein/protein interactions of Kindlin-3 give insight into its role. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.