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Structural basis for p300 Taz2-p53 TAD binding and modulation by phosphorylation

Tuesday, October 25, 2011 — Poster Session II

Noon – 2:00 p.m.

Natcher Conference Center

NCI

STRUCTBIO-2

Authors

  • H Feng
  • L Jenkins
  • S Durell
  • R Hayashi
  • S Mazur
  • S Cherry
  • J Tropea
  • M Miller
  • A Wlodawer
  • E Appella
  • Y Bai

Abstract

The CCR Molecular Modeling Core assists experimentalists across NIH by providing a structural framework for interpreting results and designing new experiments. As an example, we provide results of a study examining the interaction of the transactivating domain of the anti-tumor protein p53 with the Taz2 domain of p300 (a histone acetyltransferase coactivator). The model explains the experimentally observed effects of post-translational phosphorylation on binding affinity. The contact for the core is Stewart Durell: Stewart_Durell@nih.gov, (301) 402-4940.

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