Structural basis and kinetics of force-induced conformational changes of an αA domain-containing integrin.

ABSTRACT:

Background

Integrin α(L)β₂ (lymphocyte function-associated antigen, LFA-1) bears force upon binding to its ligand intercellular adhesion molecule 1 (ICAM-1) when a leukocyte adheres to vascular endothelium or an antigen presenting cell (APC) during immune responses. The ligand binding propensity of LFA-1 is related to its conformations, which can be regulated by force. Three conformations of the LFA-1 αA domain, determined by the position of its α₇-helix, have been suggested to correspond to three different affinity states for ligand binding.

Methodology/principal findings

The kinetics of the force-driven transitions between these conformations has not been defined and dynamically coupled to the force-dependent dissociation from ligand. Here we show, by steered molecular dyn

SUBMITTER: Xiang X 

PROVIDER: S-EPMC3225382 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature