Ontology highlight
ABSTRACT:
SUBMITTER: Klein BJ
PROVIDER: S-EPMC6212594 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
Klein Brianna J BJ Vann Kendra R KR Andrews Forest H FH Wang Wesley W WW Zhang Jibo J Zhang Yi Y Beloglazkina Anastasia A AA Mi Wenyi W Li Yuanyuan Y Li Haitao H Shi Xiaobing X Kutateladze Andrei G AG Strahl Brian D BD Liu Wenshe R WR Kutateladze Tatiana G TG
Nature communications 20181101 1
The YEATS domain has been identified as a reader of histone acylation and more recently emerged as a promising anti-cancer therapeutic target. Here, we detail the structural mechanisms for π-π-π stacking involving the YEATS domains of yeast Taf14 and human AF9 and acylated histone H3 peptides and explore DNA-binding activities of these domains. Taf14-YEATS selects for crotonyllysine, forming π stacking with both the crotonyl amide and the alkene moiety, whereas AF9-YEATS exhibits comparable affi ...[more]