Article
Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1.
The Journal of biological chemistry - 6 Dec 2002
Ceulemans Hugo, Vulsteke Veerle, De Maeyer Marc, Tatchell Kelly, Stalmans Willy, Bollen Mathieu
Abstract excerpt
Functional studies of the protein phosphatase-1 (PP1) regulator Sds22 suggest that it is indirectly and/or directly involved in one of the most ancient functions of PP1, i.e. reversing phosphorylation by the Aurora-related protein kinases. We predict that the conserved portion of Sds22 folds into a curved superhelix and demonstrate that mutation to alanine of any of eight residues (Asp(148), Phe(170), Glu(192),...
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