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TitleThe BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 7160-7175, Year 2018
Publish dateOct 28, 2017 (structure data deposition date)
AuthorsWai, D.C.C. / Szyszka, T.N. / Campbell, A.E. / Kwong, C. / Wilkinson-White, L.E. / Silva, A.P.G. / Low, J.K.K. / Kwan, A.H. / Gamsjaeger, R. / Chalmers, J.D. ...Wai, D.C.C. / Szyszka, T.N. / Campbell, A.E. / Kwong, C. / Wilkinson-White, L.E. / Silva, A.P.G. / Low, J.K.K. / Kwan, A.H. / Gamsjaeger, R. / Chalmers, J.D. / Patrick, W.M. / Lu, B. / Vakoc, C.R. / Blobel, G.A. / Mackay, J.P.
External linksJ. Biol. Chem. / PubMed:29567837
MethodsNMR (solution)
Structure data

PDB-6bgg:
Solution NMR structures of the BRD3 ET domain in complex with a CHD4 peptide
Method: SOLUTION NMR

PDB-6bgh:
Solution NMR structure of Brd3 ET domain bound to Brg1 peptide
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / transcription regulation / epigenetics / TRANSCRIPTION / Transcription Bromodomain BET protein

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