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Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion
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Published on: February 11, 2022

Complete integrin headpiece opening in eight steps.

Jieqing Zhu1, Jianghai Zhu, Timothy A Springer

  • 1Department of Biological Chemistry and Molecular Pharmacology, Program in Cellular and Molecular Medicine, Children's Hospital Boston, Harvard Medical School, Boston, MA 02115, USA.

The Journal of Cell Biology
|June 27, 2013
PubMed
Summary
This summary is machine-generated.

This study reveals the step-by-step conformational changes of the αIIbβ3 integrin headpiece when bound to Arg-Gly-Asp (RGD) peptides. These detailed atomic insights explain how integrin activation increases ligand binding affinity.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Integrins are crucial cell surface receptors mediating cell adhesion and signaling.
  • The αIIbβ3 integrin plays a key role in platelet aggregation.
  • Understanding integrin conformational changes is vital for drug development.

Purpose of the Study:

  • To capture and define distinct RGD-bound conformations of the αIIbβ3 integrin headpiece.
  • To elucidate the atomic mechanism of conformational change transmission within integrins.
  • To correlate structural changes with ligand binding affinity.

Main Methods:

  • Crystallography of αIIbβ3 integrin headpiece soaked with Arg-Gly-Asp (RGD) peptides.
  • Analysis of eight distinct RGD-bound conformations.
  • Tracing atomic movements from ligand binding site to distal domains.

Main Results:

  • Observed a transition from closed to fully open βI domain conformations, including six intermediate states.
  • Identified the sequential movement of structural elements, including the β1-α1 backbone, hybrid domain, and associated helices and loops.
  • Demonstrated long-range conformational change transmission (40 Å to 80 Å) and RGD peptide ordering within the binding groove.
  • Inferred a >200-fold increase in binding affinity upon integrin opening.

Conclusions:

  • Provided atomic-level detail of integrin headpiece conformational changes upon RGD binding.
  • Established a mechanism for how conformational changes propagate across the integrin structure.
  • Linked the energetic cost of integrin opening to a significant increase in ligand binding affinity.