6HPZ
Crystal structure of ENL (MLLT1) in complex with acetyllysine
Summary for 6HPZ
| Entry DOI | 10.2210/pdb6hpz/pdb |
| Related | 6HPW 6HPX 6HPY 6HQ0 |
| Descriptor | Protein ENL, 1,2-ETHANEDIOL, N(6)-ACETYLLYSINE, ... (4 entities in total) |
| Functional Keywords | yeats domain, inhibitor complex, structural genomics, structural genomics consortium, sgc, transcription |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18624.44 |
| Authors | Heidenreich, D.,Chaikuad, A.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2018-09-22, release date: 2018-11-28, Last modification date: 2024-01-24) |
| Primary citation | Heidenreich, D.,Moustakim, M.,Schmidt, J.,Merk, D.,Brennan, P.E.,Fedorov, O.,Chaikuad, A.,Knapp, S. Structure-Based Approach toward Identification of Inhibitory Fragments for Eleven-Nineteen-Leukemia Protein (ENL). J.Med.Chem., 61:10929-10934, 2018 Cited by PubMed Abstract: Lysine acetylation is an epigenetic mark that is principally recognized by bromodomains, and recently structurally diverse YEATS domains also emerged as readers of lysine acetyl/acylations. Here we present a crystallography-based strategy and the discovery of fragments binding to the ENL YEATS domain, a potential drug target. Crystal structures combined with synthetic efforts led to the identification of a submicromolar binder, providing first starting points for the development of chemical probes for this reader domain family. PubMed: 30407816DOI: 10.1021/acs.jmedchem.8b01457 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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