Uhart, Marina; Iglesias, Alberto A.; Bustos, Diego M.
Structurally Constrained Residues Outside the Binding Motif Are Essential in the Interaction of 14-3-3 and Phosphorylated Partner
JOURNAL OF MOLECULAR BIOLOGY, 406:552-557, MAR 4 2011

14-3-3 proteins participate in many key cellular processes after binding to disordered phospho-partners. Usually, the phosphorylated state is an essential target for the binding. Here, we show for the first time residues other than those in the 14-3-3 binding motif that are essential for the binding between 14-3-3 and a phosphorylated partner. Results support that phosphorylation, although necessary, is not sufficient for 14-3-3's complex formation, as structurally constrained anchor residues play a critical function in stabilizing the protein protein interaction. (C) 2011 Elsevier Ltd. All rights reserved.

DOI:10.1016/j.jmb.2010.12.043

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