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14-3-3 Domain
Class:Phospho-Ser binding
Structure:

No Image Crystal structures of the mammalian tau and epsilon isoforms of the 14-3-3 module show that each module is composed of nine anti-parallel alpha helices. Dimerization results in the formation of a negatively charged channel between the two monomers. This channel is lined with invariant residues that mediate interactions with a phosphoserine peptide target sequence. The figure shows the 14-3-3 x dimer complexed with phosphoserine peptide containing the 14-3-3 binding motif.

Structure Reference: PDB: 2B05.

Domain binding and function:
14-3-3 genes encode a ubiquitous family of highly conserved proteins of ~30 kDa acidic proteins found in eukaryotic lineages as diverse as fungi, plants and animals.  Mammals encode seven closely related members (β, γ, ε, η, σ, τ, and ζ).  Implicated in a wide variety of cellular processes such as apoptosis, stress response and cell cycle, their most notable function is to bind to phosphoserine/phosphothreonine motifs in a sequence-specific manner. The structure of 14-3-3 consists of a tertiary structure consisting of nine α-helices for each monomer, with the biologically functional dimer resembling a U shaped structure. 14-3-3 proteins have been linked to a number of diseases such as cancer, Cruezfeldt-Jacob disease, Alzheimers, and Miller-Dieker syndrome.

 

Examples of Proteins: 

Binding partner
Function Links
Cdc25 tyrosine phosphatase  Cell cycle regulation  ELM
BAD (Bcl-XL binding partner)  Regulation of apotosis  SMART
c-Raf Ser/Thr Kinase  Regulation of kinase activity; Signal transduction  Pfam
PKC Ser/Thr Kinase  Signal transduction  GlobPlot
MEKK1,2,3 Ser/Thr Kinase  Signal transduction  




Consensus Binding Sites



R-X-[Ar/S]-[+]-pS-[LEAM]-P or R-[S/Ar]-[+]-pS-[LEAM]-P

Where Ar=aromatic residue, [+]=basic residue and pS=phosphoserine





No Image


 
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