Key interactions in integrin ectodomain responsible for global conformational change detected by elastic network normal-mode analysis.

ABSTRACT: Integrin, a membrane protein with a huge extracellular domain, participates in cell-cell and cell-extracellular-matrix interactions for metazoan. A group of integrins is known to perform a large-scale structural change when the protein is activated, but the activation mechanism and generality of the conformational change remain to be elucidated. We performed normal-mode analysis of the elastic network model on integrin alpha(V)beta(3) ectodomain in the bent form and identified key residues that influenced molecular motions. Iterative normal-mode calculations demonstrated that the specific nonbonded interactions involving the key residues work as a snap to keep integrin in the bent form. The importance of the key residues for the conformational change was further verified by mutation experi

SUBMITTER: Matsumoto A 

PROVIDER: S-EPMC2527288 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature