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TitleStructural mechanism of BRD4-NUT and p300 bipartite interaction in propagating aberrant gene transcription in chromatin in NUT carcinoma.
Journal, issue, pagesNat Commun, Vol. 14, Page 378-378, Year 2023
Publish dateMar 31, 2022 (structure data deposition date)
AuthorsYu, D. / Liang, Y. / Kim, C. / Jaganathan, A. / Ji, D. / Han, X. / Yang, X. / Jia, Y. / Gu, R. / Wang, C. ...Yu, D. / Liang, Y. / Kim, C. / Jaganathan, A. / Ji, D. / Han, X. / Yang, X. / Jia, Y. / Gu, R. / Wang, C. / Zhang, Q. / Cheung, K.L. / Zhou, M.M. / Zeng, L.
External linksNat Commun / PubMed:36690674
MethodsNMR (solution)
Structure data

PDB-7xez:
NMR solution structures of p300 TAZ2 domain in complex with BRD4-NUT F1c domain binding motif #2
Method: SOLUTION NMR

PDB-7xfg:
NMR solution structures of p300 TAZ2 domain in complex with BRD4-NUT F1c domain binding motif #1
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / BRD4-NUT fusion protein / CBP/p300 / TAZ2 domain / F1c domain / NUT carcinoma / PEPTIDE BINDING PROTEIN

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