Structure and binding interface of the cytosolic tails of αXβ2 integrin.

ABSTRACT:

Background

Integrins are signal transducer proteins involved in a number of vital physiological processes including cell adhesion, proliferation and migration. Integrin molecules are hetero-dimers composed of two distinct subunits, α and β. In humans, 18 α and 8 β subunits are combined into 24 different integrin molecules. Each of the subunit comprises a large extracellular domain, a single pass transmembrane segment and a cytosolic tail (CT). The CTs of integrins are vital for bidirectional signal transduction and in maintaining the resting state of the receptors. A large number of intracellular proteins have been found to interact with the CTs of integrins linking integrins to the cytoskeleton.

Methodology/principal findings

In this work, we have investigated structure and

SUBMITTER: Chua GL 

PROVIDER: S-EPMC3406025 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature