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Structural basis for ligand recognition by integrins.

Junichi Takagi¹

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

Current Opinion in Cell Biology

|October 19, 2007

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Integrins are key cell surface receptors for cell-adhesion. Structural studies reveal two distinct binding surfaces, explaining how integrins recognize diverse ligands for multicellular life.

Area of Science:

Cell Biology
Structural Biology
Evolutionary Biology

Background:

Integrins are essential cell surface receptors mediating cell-extracellular matrix (ECM) adhesion in all multicellular organisms.
Evolutionary increases in animal complexity necessitated integrins acquiring diverse recognition capabilities for various ECM ligands and cell surface receptors.

Purpose of the Study:

To elucidate the structural basis of integrin-ligand interactions.
To understand how integrins achieve specific recognition of a wide variety of ligands.

Main Methods:

Structural determination of integrin-ligand complexes for both I domain-containing and non-I domain-containing integrins.
Biochemical and pharmacological characterization of integrin-ligand interactions.

Related Experiment Videos

Main Results:

Revealed two fundamentally different types of integrin-binding surfaces.
Identified a small binding cleft at the subunit interface common to all integrins as crucial for ligand recognition.

Conclusions:

The structural diversity of integrin-binding surfaces and the conserved binding cleft explain integrins' ability to recognize numerous ligands.
These findings are central to understanding the physiology of multicellular organisms and potential therapeutic targets.