Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and phosphorylated partner.

Abstract:

: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.

journal_name

J Mol Biol

authors

Uhart M,Iglesias AA,Bustos DM

doi

10.1016/j.jmb.2010.12.043

subject

Has Abstract

pub_date

2011-03-04 00:00:00

pages

552-7

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(11)00002-7

journal_volume

406

pub_type

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