NMR structure of integrin α4 cytosolic tail and its interactions with paxillin.

ABSTRACT:

Background

Integrins are a group of transmembrane signaling proteins that are important in biological processes such as cell adhesion, proliferation and migration. Integrins are α/β hetero-dimers and there are 24 different integrins formed by specific combinations of 18 α and 8 β subunits in humans. Generally, each of these subunits has a large extracellular domain, a single pass transmembrane segment and a cytosolic tail (CT). CTs of integrins are important in bidirectional signal transduction and they associate with a large number of intracellular proteins.

Principal findings

Using NMR spectroscopy, we determined the 3-D structure of the full-length α4 CT (Lys968-Asp999) and characterize its interactions with the adaptor protein paxillin. The α4 CT assumes an overall helic

SUBMITTER: Chua GL 

PROVIDER: S-EPMC3561355 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature