Ontology highlight
ABSTRACT:
SUBMITTER: Watson PJ
PROVIDER: S-EPMC4848466 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Watson Peter J PJ Millard Christopher J CJ Riley Andrew M AM Robertson Naomi S NS Wright Lyndsey C LC Godage Himali Y HY Cowley Shaun M SM Jamieson Andrew G AG Potter Barry V L BV Schwabe John W R JW
Nature communications 20160425
Histone deacetylases (HDACs) 1, 2 and 3 form the catalytic subunit of several large transcriptional repression complexes. Unexpectedly, the enzymatic activity of HDACs in these complexes has been shown to be regulated by inositol phosphates, which bind in a pocket sandwiched between the HDAC and co-repressor proteins. However, the actual mechanism of activation remains poorly understood. Here we have elucidated the stereochemical requirements for binding and activation by inositol phosphates, de ...[more]