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Relating conformation to function in integrin α5β1.

Yang Su1, Wei Xia1, Jing Li1

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

Proceedings of the National Academy of Sciences of the United States of America
|June 19, 2016
PubMed
Summary
This summary is machine-generated.

This study characterizes β1 integrin ectodomain conformations, revealing that extended-open states are adhesive, while closed states are not. Antibodies stabilize specific conformations, influencing cell adhesion to fibronectin.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • β1 integrins are crucial for cell adhesion, but their conformational states and how antibodies affect them are not fully understood.
  • Understanding β1 integrin conformations is key to deciphering their role in cellular processes.

Purpose of the Study:

  • To characterize the conformational states of the α5β1 integrin ectodomain.
  • To determine how different antibodies stabilize specific α5β1 conformations.
  • To correlate these conformations with cellular adhesion function.

Main Methods:

  • Negative-stain electron microscopy was used to visualize α5β1 ectodomain structures.
  • Antibody binding sites and their effects on conformation were analyzed.
  • Cell adhesion assays were performed to assess functional consequences.

Main Results:

  • The α5β1 ectodomain adopts extended-closed, extended-open, and bent conformations.
  • Activating antibodies stabilize extended conformations, while inhibitory antibodies stabilize closed conformations.
  • The extended-open conformation correlates with cell adhesion to fibronectin.

Conclusions:

  • Antibodies can modulate α5β1 integrin conformation and function.
  • Specific α5β1 conformations dictate cell adhesion to fibronectin.
  • This work provides insights into integrin allosteric regulation and function.