TY  - INPR
A1  - Ni, Xiaomin
A1  - Heidenreich, David Jonas
A1  - Christott, Thomas
A1  - Bennett, James
A1  - Moustakim, Moses
A1  - Brennan, Paul E.
A1  - Fedorov, Oleg
A1  - Knapp, Stefan
A1  - Chaikuad, Apirat
T1  - Structural insights into interaction mechanisms of alternative piperazine-urea YEATS domain binders in MLLT1
T2  - bioRxiv
N2  - 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.
Y1  - 2019
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/72658
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-726581
IS  - 836932
ER  -