5A0O
adhiron raised against p300
Summary for 5A0O
| Entry DOI | 10.2210/pdb5a0o/pdb |
| Descriptor | ADHIRON (2 entities in total) |
| Functional Keywords | de novo protein, affimer |
| Biological source | SYNTHETIC CONSTRUCT |
| Total number of polymer chains | 2 |
| Total formula weight | 24930.49 |
| Authors | 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. (deposition date: 2015-04-21, release date: 2015-07-15, Last modification date: 2024-01-10) |
| Primary citation | 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. Exploration of the Hif-1Alpha.P300 Interface Using Peptide and Adhiron Phage Display Technologies Mol.Biosyst., 11:2738-, 2015 Cited by 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. PubMed: 26135796DOI: 10.1039/C5MB00284B PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.73 Å) |
Structure validation
Download full validation report
