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Integrin activation and structural rearrangement.

Junichi Takagi1, Timothy A Springer

  • 1The Center for Blood Research, Department of Pathology, Harvard Medical School, Boston 02115, Massachusetts, USA.

Immunological Reviews
|September 18, 2002
PubMed
Summary
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Integrin activation involves conformational changes, particularly in the I domain, switching between low-affinity closed and high-affinity open states. This mechanism, similar to G-proteins, enables rapid cell adhesion during inflammation and injury.

Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Integrins are crucial adhesion receptors regulating cell adhesion and de-adhesion.
  • Rapid activation of beta2 integrins on leukocytes and beta3 integrins on platelets is vital for immune response and hemostasis.

Purpose of the Study:

  • To elucidate a unifying mechanism for integrin activation, encompassing both I domain-containing and I domain-lacking integrins.
  • To explain the structural basis for rapid integrin activation and ligand binding.

Main Methods:

  • Analysis of crystal, nuclear magnetic resonance (NMR), and electron microscope (EM) structures of integrins and their domains.
  • Functional studies and mutational analysis to assess the impact of conformational states on ligand affinity.

Related Experiment Videos

Main Results:

  • A unified mechanism of integrin activation is proposed, involving two I domain conformations: closed (low affinity) and open (high affinity).
  • Rearrangement of a Mg2+-binding site, analogous to G-proteins, triggers large conformational shifts.
  • The open conformation, facilitated by C-terminal alpha-helix movement, increases ligand-binding affinity up to 9,000-fold.
  • Integrin headpiece rearrangements, including beta-propeller, I, and I-like domains, and EGF domains in the stalk, contribute to activation.

Conclusions:

  • Integrin activation involves a switchblade-like opening of the headpiece, driven by long-range structural rearrangements.
  • Conformational changes within I and I-like domains are intrinsically linked to the overall molecular activation, enhancing ligand-binding competence.