Distinct recognition of complement iC3b by integrins α_Xβ₂ and α_Mβ₂.

ABSTRACT: Recognition by the leukocyte integrins α_Xβ₂ and α_Mβ₂ of complement iC3b-opsonized targets is essential for effector functions including phagocytosis. The integrin-binding sites on iC3b remain incompletely characterized. Here, we describe negative-stain electron microscopy and biochemical studies of α_Xβ₂ and α_Mβ₂ in complex with iC3b. Despite high homology, the two integrins bind iC3b at multiple distinct sites. α_Xβ₂ uses the α_X αI domain to bind iC3b on its C3c moiety at one of two sites: a major site at the interface between macroglobulin (MG) 3 and MG4 domains, and a less frequently used site near the C345C domain. In contrast, α_Mβ₂ uses its αI do

SUBMITTER: Xu S 

PROVIDER: S-EPMC5380021 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature