Structural Characterization of the Interaction between the α_MI-Domain of the Integrin Mac-1 (α_Mβ₂) and the Cytokine Pleiotrophin.

ABSTRACT: Integrin Mac-1 (α_Mβ₂) is an adhesion receptor vital to many functions of myeloid leukocytes. It is also the most promiscuous member of the integrin family capable of recognizing a broad range of ligands. In particular, its ligand-binding α_MI-domain is known to bind cationic proteins/peptides depleted in acidic residues. This contradicts the canonical ligand-binding mechanism of αI-domains, which requires an acidic amino acid in the ligand to coordinate the divalent cation within the metal ion-dependent adhesion site (MIDAS) of αI-domains. The lack of acidic amino acids in the α_MI-domain-binding sequences suggests the existence of an as-yet uncharacterized interaction mechanism. In the present study, we analyzed interactions of the α_MI-

SUBMITTER: Feng W 

PROVIDER: S-EPMC8641143 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature