Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation

@article{Delvecchio2013StructureOT,
  title={Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation},
  author={Manuela Delvecchio and Jonathan Gaucher and Carmen Aguilar-Gurrieri and Esther Ortega and Daniel Panne},
  journal={Nature Structural &Molecular Biology},
  year={2013},
  volume={20},
  pages={1040-1046}
}
CBP and p300 are histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. Mutations in their catalytic 'cores' are linked to genetic disorders, including cancer. Here we present the 2.8-Å crystal structure of the catalytic core of human p300 containing its bromodomain, CH2 region and HAT domain. The structure reveals that the CH2 region contains a discontinuous PHD domain interrupted by a RING domain. The bromodomain, PHD, RING and HAT… CONTINUE READING
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