Magnesium Activates Microsecond Dynamics to Regulate Integrin-Collagen Recognition.

ABSTRACT: Integrin receptors bind collagen via metal-mediated interactions that are modulated by magnesium (Mg²⁺) levels in the extracellular matrix. Nuclear magnetic resonance-based relaxation experiments, isothermal titration calorimetry, and adhesion assays reveal that Mg²⁺ functions as both a structural anchor and dynamic switch of the α₁β₁ integrin I domain (α₁I). Specifically, Mg²⁺ binding activates micro- to millisecond timescale motions of residues distal to the binding site, particularly those surrounding the salt bridge at helix 7 and near the metal ion-dependent adhesion site. Mutagenesis of these residues impacts α₁I functional activity, thereby suggesting that Mg-bound α₁I dynamics are important for

SUBMITTER: Nunes AM 

PROVIDER: S-EPMC6615728 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature