The importance of N-glycosylation on β₃ integrin ligand binding and conformational regulation.

ABSTRACT: N-glycosylations can regulate the adhesive function of integrins. Great variations in both the number and distribution of N-glycosylation sites are found in the 18 α and 8 β integrin subunits. Crystal structures of α_IIbβ₃ and α_Vβ₃ have resolved the precise structural location of each N-glycan site, but the structural consequences of individual N-glycan site on integrin activation remain unclear. By site-directed mutagenesis and structure-guided analyses, we dissected the function of individual N-glycan sites in β₃ integrin activation. We found that the N-glycan site, β₃-N320 at the headpiece and leg domain interface positively regulates α_IIbβ₃ but not α_Vβ₃ activation. The β_3</

SUBMITTER: Cai X 

PROVIDER: S-EPMC5498496 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature