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Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
Published on: February 15, 2018
Structural basis for ligand recognition by integrins
1Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan. takagi@protein.osaka-u.ac.jp
Abstract:
Integrins, the major cell surface receptors mediating cell-extracellular matrix (ECM) adhesion, are central to the basic physiology underlying all multicellular organisms. As the complexity of animal body architecture increased, integrins were forced to acquire recognition capabilities toward the wide variety of ECM ligands and cell surface counter-receptors that emerged during evolution. Structural determination of the integrin-ligand complexes for both I domain-containing and non-I domain-containing integrins revealed two fundamentally different types of integrin-binding surfaces. In addition, recent advances in the biochemical and pharmacological characterization of the integrin-ligand interactions are beginning to reveal how integrins achieve specific recognition of wide variety of ligands using a small binding cleft at the subunit interface common to all integrins.
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