6T1O
Crystal structure of MLLT1 (ENL) YEATS domain in complexed with benzimidazole-amide derivative 6
Summary for 6T1O
| Entry DOI | 10.2210/pdb6t1o/pdb |
| Descriptor | Protein ENL, 4-iodanyl-~{N}-[2-(piperidin-1-ylmethyl)-3~{H}-benzimidazol-5-yl]benzamide, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | transcription, yeats domain, enl, mllt1, chemical probe, inhibitor, structural genomics, structural genomics consortium, sgc |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18995.65 |
| Authors | Chaikuad, A.,Heidenreich, D.,Moustakim, M.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Fedorov, O.,Brennan, P.E.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2019-10-04, release date: 2019-11-06, Last modification date: 2024-01-24) |
| Primary citation | Ni, X.,Heidenreich, D.,Christott, T.,Bennett, J.,Moustakim, M.,Brennan, P.E.,Fedorov, O.,Knapp, S.,Chaikuad, A. Structural Insights into Interaction Mechanisms of Alternative Piperazine-urea YEATS Domain Binders in MLLT1. Acs Med.Chem.Lett., 10:1661-1666, 2019 Cited by PubMed Abstract: YEATS-domain-containing MLLT1 is an acetyl/acyl-lysine reader domain, which is structurally distinct from well-studied bromodomains and has been strongly associated in development of cancer. Here, we characterized piperazine-urea derivatives as an acetyl/acyl-lysine mimetic moiety for MLLT1. Crystal structures revealed distinct interaction mechanisms of this chemotype compared to the recently described benzimidazole-amide based inhibitors, exploiting different binding pockets within the protein. Thus, the piperazine-urea scaffold offers an alternative strategy for targeting the YEATS domain family. PubMed: 31857843DOI: 10.1021/acsmedchemlett.9b00460 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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