Mechanically Regulated Outside-In Activation of an I-Domain-Containing Integrin.

ABSTRACT: Integrins are heterodimeric transmembrane proteins that mediate cellular adhesion and bidirectional mechanotransductions through their conformational allostery. The allosteric pathway of an I-domain-containing integrin remains unclear because of its complexity and lack of effective experiments. For a typical I-domain-containing integrin α_Xβ₂, molecular dynamics simulations were employed here to investigate the conformational dynamics in the first two steps of outside-in activation, the bindings of both the external and internal ligands. Results showed that the internal ligand binding is a prerequisite to the allosteric transmission from the α- to β-subunits and the exertion of external force to integrin-ligand complex. The opening state of αI domain with downward move

SUBMITTER: Mao D 

PROVIDER: S-EPMC7474184 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature