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Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies

DOI: 10.1039/C5MB00284B DOI Help
PMID: 26135796 PMID Help

Authors: Hannah F. Kyle (University of Leeds) , Kate F. Wickson (AstraZeneca Discovery Sciences) , Jonathan Stott (AstraZeneca Discovery Sciences) , George M. Burslem (University of Leeds) , Alexander L. Breeze (University of Leeds) , Christian Tiede (University of Leeds) , Darren C. Tomlinson (University of Leeds) , Stuart L. Warriner (University of Leeds) , Adam Nelson (University of Leeds) , Andrew J. Wilson (University of Leeds) , Thomas A. Edwards (University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Mol. Biosyst. , VOL 11 , PAGES 2738 - 2749

State: Published (Approved)
Published: June 2015

Abstract: The HIF-1 alpha/p300 protein-protein interaction plays a key role in tumor metabolism and thus represents a high value target for anticancer drug-development. Although several studies have identified inhibitor candidates using rationale design, more detailed understanding of the interaction and binding interface is necessary to inform development of superior inhibitors. In this work, we report a detailed biophysical analysis of the native interaction with both peptide and Adhiron phage display experiments to identify novel binding motifs and binding regions of the surface of p300 to inform future inhibitor design.

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

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