Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension.

ABSTRACT: Integrins are conformationally flexible cell surface receptors that survey the extracellular environment for their cognate ligands. Interactions with ligands are thought to be linked to global structural rearrangements involving transitions between bent, extended-closed and extended-open forms. Thus far, structural details are lacking for integrins in the extended conformations due to extensive flexibility between the headpiece and legs in this conformation. Here we present single-particle electron cryomicroscopy structures of human αvβ8 integrin in the extended-closed conformation, which has been considered to be a low-affinity intermediate. Our structures show the headpiece rotating about a flexible αv knee, suggesting a ligand surveillance mechanism for integrins in their extended-close

SUBMITTER: Cormier A 

PROVIDER: S-EPMC6214843 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature