Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase

Intrinsically disordered proteins can form highly dynamic complexes with partner proteins. One such dynamic complex involves the intrinsically disordered Sic1 with its partner Cdc4 in regulation of yeast cell cycle progression. Phosphorylation of six N-terminal Sic1 sites leads to equilibrium engage...

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Bibliografiske detaljer
Main Authors:	Mittag, Tanja, Marsh, Joseph, Grishaev, Alexander, Orlicky, Stephen, Lin, Hong, Sicheri, Frank, Tyers, Mike, Forman-Kay, Julie D.
Format:	Artigo
Sprog:	Inglês
Udgivet:	2010
Fag:	Article
Online adgang:	https://ncbi.nlm.nih.gov/pmc/articles/PMC2924144/ https://ncbi.nlm.nih.gov/pubmed/20399186 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2010.01.020
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Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase

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