Journal
MOLECULAR BIOSYSTEMS
Volume 11, Issue 10, Pages 2738-2749Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5mb00284b
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Funding
- AstraZeneca
- EPSRC
- European Research Council [ERC-StG-240324]
- Wellcome Trust [094232]
- BBSRC [BB/L015056/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L015056/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1090344] Funding Source: researchfish
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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.
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