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-Structure paper
Title | Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 109, Page 3287-3292, Year 2012 |
Publish date | Dec 20, 2011 (structure data deposition date) |
![]() | Tang, X. / Orlicky, S. / Mittag, T. / Csizmok, V. / Pawson, T. / Forman-Kay, J.D. / Sicheri, F. / Tyers, M. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.306 Å |
Structure data | ![]() PDB-3v7d: |
Chemicals | ![]() ChemComp-HOH: |
Source |
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![]() | CELL CYCLE / WD 40 domain / phospho-peptide complex / E3 ubiquitin ligase / ligase / phospho binding protein / Sic1 / phosphorylation |