The connection between metal ion affinity and ligand affinity in integrin I domains.

ABSTRACT: Integrins are cell-surface heterodimeric proteins that mediate cell-cell, cell-matrix, and cell-pathogen interactions. Half of the known integrin alpha subunits contain inserted domains (I domains) that coordinate ligand through a metal ion. Although the importance of conformational changes within isolated I domains in regulating ligand binding has been reported, the relationship between metal ion binding affinity and ligand binding affinity has not been elucidated. Metal and ligand binding by several I domain mutants that are stabilized in different conformations are investigated using isothermal titration calorimetry and surface plasmon resonance studies. This work suggests an inverse relationship between metal ion affinity and ligand binding affinity (i.e. constructs with a high affinit

SUBMITTER: Vorup-Jensen T 

PROVIDER: S-EPMC2040231 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature