Autonomous conformational regulation of β₃ integrin and the conformation-dependent property of HPA-1a alloantibodies.

ABSTRACT: Integrin α/β heterodimer adopts a compact bent conformation in the resting state, and upon activation undergoes a large-scale conformational rearrangement. During the inside-out activation, signals impinging on the cytoplasmic tail of β subunit induce the α/β separation at the transmembrane and cytoplasmic domains, leading to the extended conformation of the ectodomain with the separated leg and the opening headpiece that is required for the high-affinity ligand binding. It remains enigmatic which integrin subunit drives the bent-to-extended conformational rearrangement in the inside-out activation. The β₃ integrins, including α_IIbβ₃ and α_Vβ₃, are the prototypes for understanding integrin structural regulation. The Leu33Pro polymorphis

SUBMITTER: Thinn AMM 

PROVIDER: S-EPMC6166792 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature