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TitleStructural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays.
Journal, issue, pagesJ. Mol. Biol., Vol. 393, Page 409-424, Year 2009
Publish dateMay 8, 2009 (structure data deposition date)
AuthorsMurphy, J.M. / Hansen, D.F. / Wiesner, S. / Muhandiram, D.R. / Borg, M. / Smith, M.J. / Sicheri, F. / Kay, L.E. / Forman-Kay, J.D. / Pawson, T.
External linksJ. Mol. Biol. / PubMed:19715701
MethodsNMR (solution)
Structure data

PDB-2kis:
Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION REGULATOR / FF domain / extended helix / interdomain helix / linker peptide / interdomain dynamics / Activator / Alternative splicing / Coiled coil / Nucleus / Phosphoprotein / Repressor / Transcription / Transcription regulation

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