Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand.

ABSTRACT: The affinity of the extracellular domain of integrins for ligand is regulated by conformational changes signaled from the cytoplasm. Alternative types of conformational movement in the ligand-binding headpiece have been proposed. In one study, electron micrograph image averages of the headpiece of integrin aV beta 3 show two different conformations. The open conformation of the headpiece is present when a ligand mimetic peptide is bound and differs from the closed conformation in the presence of an obtuse angle between the beta 3 subunit hybrid and I-like domains. We tested the hypothesis that opening of the hybrid-I-like domain interface increases ligand-binding affinity by mutationally introducing an N-glycosylation site into it. Both beta 3 and beta1 integrin glycan wedge mutants exhibi

SUBMITTER: Luo BH 

PROVIDER: S-EPMC151353 | biostudies-literature | 2003 Mar

REPOSITORIES: biostudies-literature