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Structure paper

TitleComposite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 109, Page 3287-3292, Year 2012
Publish dateDec 20, 2011 (structure data deposition date)
AuthorsTang, X. / Orlicky, S. / Mittag, T. / Csizmok, V. / Pawson, T. / Forman-Kay, J.D. / Sicheri, F. / Tyers, M.
External linksProc. Natl. Acad. Sci. USA / PubMed:22328159
MethodsX-ray diffraction
Resolution2.306 Å
Structure data

PDB-3v7d:
Crystal Structure of ScSkp1-ScCdc4-pSic1 peptide complex
Method: X-RAY DIFFRACTION / Resolution: 2.306 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCELL CYCLE / WD 40 domain / phospho-peptide complex / E3 ubiquitin ligase / ligase / phospho binding protein / Sic1 / phosphorylation

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