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TitleNMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding.
Journal, issue, pagesJ. Mol. Biol., Vol. 389, Page 230-237, Year 2009
Publish dateSep 2, 2008 (structure data deposition date)
AuthorsBonet, R. / Ruiz, L. / Aragon, E. / Martin-Malpartida, P. / Macias, M.J.
External linksJ. Mol. Biol. / PubMed:19393245
MethodsNMR (solution)
Structure data

PDB-2k85:
p190-A RhoGAP FF1 domain
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / FF domain / p190-A RhoGAP / protein phosphorylation / Alternative splicing / Anti-oncogene / Cell cycle / Cytoplasm / DNA-binding / GTPase activation / Nucleus / Phosphoprotein / Repressor / Transcription / Transcription regulation

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