Title : Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.

Pub. Date : 2001 Jul 24

PMID : 11456485






1 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Ess1 WW folds and unfolds reversibly, but in the absence of ligand is only marginally stable with a melting temperature of 19 degrees C. The WW domain is stabilized by the addition of anionic ligands, namely, chloride, inorganic phosphate, phosphoserine, and phosphorylated CTD peptides. Phosphoserine peptidylprolyl isomerase ESS1 Saccharomyces cerevisiae S288C