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

Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response.

Sonja A Dames1, Maria Martinez-Yamout, Roberto N De Guzman

  • 1Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Proceedings of the National Academy of Sciences of the United States of America
|April 18, 2002
PubMed
Summary

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

Quantifying species-specific binding affinities of transthyretin aggregation inhibitors.

Biophysical reports·2026
Same author

Discovery of a Cryptic Pocket in EcDsbA Opens New Opportunities for Antibacterial Discovery.

Angewandte Chemie (International ed. in English)·2025
Same author

Linker Length and Composition within Disordered Binding Motifs Modulates the Avidity and Reversibility of a Multivalent Protein Interaction Switch.

Journal of molecular biology·2025
Same author

The type III secretion system translocases IpaC, SipC, and BipC are partially folded alpha helical proteins lacking in tertiary structures.

PloS one·2025
Same author

Mechanism of inhibition of acid-mediated transthyretin aggregation by designed peptides.

The Journal of biological chemistry·2025
Same author

Linker Length and Composition within Disordered Binding Motifs modulates the Avidity and Reversibility of a Multivalent Protein Interaction Switch.

bioRxiv : the preprint server for biology·2025

Hypoxia-inducible factor 1 (HIF-1) recruits coactivators CBP/p300 via its Hif-1 alpha subunit to adapt cells to low oxygen. This study reveals the structural basis of this critical interaction, offering insights into tumor growth regulation.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Cellular response to hypoxia is mediated by HIF-1.
  • HIF-1 recruits coactivators CBP/p300 through Hif-1 alpha.
  • Disrupting Hif-1 alpha/p300 interaction may attenuate tumor growth.

Purpose of the Study:

  • To determine the solution structure of the Hif-1 alpha CAD and CBP TAZ1 complex.
  • To delineate the structural basis of the Hif-1 alpha/p300 interaction.

Main Methods:

  • Solution structure determination of the Hif-1 alpha CAD/CBP TAZ1 complex.
  • Structural comparison of TAZ1 and TAZ2 domains.

Main Results:

  • The Hif-1 alpha CAD is intrinsically disordered and binds CBP TAZ1 by forming three short helices.

Related Experiment Videos

  • Key interactions include the hypoxic switch Asn-803 and extensive hydrophobic contacts.
  • Differences in helix packing between TAZ1 and TAZ2 contribute to specificity.

    • Conclusions:

    • The determined structure provides novel insights into Hif-1 alpha's recruitment of CBP/p300 under hypoxia.
    • Understanding this interaction mechanism is crucial for cancer research and therapeutic strategies.