Ligand binding and affinity modulation of integrins

Eileen Collins Tozer, Paul E. Hughes, Joseph C Loftus

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

Integrins are cell adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. The extracellular domains of these receptors possess binding sites for a diverse range of protein ligands. Ligand binding is divalent cation dependent and involves well-defined motifs in the ligand. Integrins can dynamically regulate their affinity for ligands (inside-out signaling). This ability to rapidly modulate their affinity state is key to their involvement in such processes as cell migration and platelet aggregation. This review will focus on two aspects of integrin function: first, on the molecular basis of ligand-integrin interactions and, second, on the underlying mechanisms controlling the affinity state of integrins for their ligands.

Original languageEnglish (US)
Pages (from-to)785-798
Number of pages14
JournalBiochemistry and Cell Biology
Volume74
Issue number6
StatePublished - 1996
Externally publishedYes

    Fingerprint

Keywords

  • Affinity modulation
  • Integrins
  • Ligand binding

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this