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 Bioljournal_title
Journal of molecular biologyauthors
Uhart M,Iglesias AA,Bustos DMdoi
10.1016/j.jmb.2010.12.043subject
Has Abstractpub_date
2011-03-04 00:00:00pages
552-7issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(11)00002-7journal_volume
406pub_type
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