Download MendeleyExploration of the Hif-1Alpha.P300 Interface Using Peptide and Adhiron Phage Display Technologies
Kyle, H.F., Wickson, K.F., Stott, J., Burslem, G.M., Breeze, A.L., Tiede, C., Tomlinson, D.C., Warriner, S.L., Nelson, A., Wilson, A.J., Edwards, T.A.(2015) Mol Biosyst 11: 2738
- PubMed: 26135796
- DOI: https://doi.org/10.1039/c5mb00284b
- Primary Citation of Related Structures:
5A0O - PubMed Abstract:
The HIF-1α/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.
Organizational Affiliation:
Astbury Centre for Structural Molecular Biology, University of Leeds, Woodhouse Lane, Leeds, LS2 9JT, UK. t.a.edwards@leeds.ac.uk.
