Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Integrin-collagen complex: a metal-glutamate handshake.

J Bella1, H M Berman

  • 1Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, Manchester, M13 9PT, UK.

Structure (London, England : 1993)
|June 30, 2000
PubMed
Summary

The crystal structure reveals how integrin I domains bind collagen peptides, confirming a known mechanism. This finding is crucial for understanding integrin activation and cell signaling pathways.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Hydroxylated anthraquinones produced by Geosmithia species.

Folia microbiologica·2009
Same author

Conformations of the sugar-phosphate backbone in helical DNA crystal structures.

Biopolymers·2009
Same author

The leucine-rich repeat structure.

Cellular and molecular life sciences : CMLS·2008
Same author

Indirect readout of DNA sequence at the primary-kink site in the CAP-DNA complex: DNA binding specificity based on energetics of DNA kinking.

Journal of molecular biology·2001
Same author

Indirect readout of DNA sequence at the primary-kink site in the CAP-DNA complex: alteration of DNA binding specificity through alteration of DNA kinking.

Journal of molecular biology·2001
Same author

A standard reference frame for the description of nucleic acid base-pair geometry.

Journal of molecular biology·2001

Area of Science:

  • Structural biology
  • Molecular biology
  • Biochemistry

Background:

  • Integrin I domains mediate cell adhesion by binding extracellular matrix proteins.
  • Collagen is a key component of the extracellular matrix, involved in cell-matrix interactions.
  • Previous models proposed a binding mechanism for integrin I domains, but lacked direct structural evidence.

Purpose of the Study:

  • To determine the crystal structure of the complex between an integrin I domain and a synthetic collagen peptide.
  • To elucidate the molecular details of collagen binding by integrin I domains.
  • To provide structural insights into integrin activation and signaling.

Main Methods:

  • X-ray crystallography to determine the 3D structure of the integrin I domain-collagen peptide complex.

Related Experiment Videos

  • Biochemical assays to characterize the binding interactions.

    • Main Results:

    • The crystal structure reveals a collagen triple-helix specifically recognized and bound by the integrin I domain.
    • The observed binding mode is consistent with the previously proposed mechanism.
    • The structure provides atomic-level details of the macromolecular recognition interface.

    Conclusions:

    • The determined structure validates the proposed binding mechanism of integrin I domains to collagen.
    • This structural information has significant implications for understanding integrin activation.
    • The findings contribute to the broader understanding of cell adhesion and signaling processes involving integrins and collagen.