YWHAB: Human brain protein 14-3-3 beta isoform
PDB Code: 2BQ0
Phosphorylation of a target protein by a specific kinase alters the characteristics of the protein in a number of ways. One alteration is that the attached phosphate group presents a handle to which other molecules can bind thus forming a complex. This is generally how the 14-3-3 molecules interact with their proteins.
14-3-3 proteins are highly conserved eukaryotic proteins that bind to phosphorylated Ser (pS) residues via the two consensus sequences of RXXXpSXP and R(S/X)XpSXP. The functional unit is a dimer and their interaction with the phosphorylated target can result in stabilisation of the protein, alteration of enzyme activity, localisation within the cell, prevention of dephosphorylation and either blockage or mediation of protein interactions.
The symmetric dimer conformation as seen for the previous 14-3-3 structures. The circles represent the locations of the peptide binding sites.
Previously the structure of the 14-3-3 proteins were believed to be rigid as the conformation of both the bound and unbound forms were essentially identical. This lead to the idea that the target proteins undergo a conformational change upon binding and that the 14-3-3 molecule remains unchanged. The 14-3-3 b structure presented here changes this view. The structure is again a dimer but this time for one of the monomers three helices, that form part of the phospho-peptide binding site, have undergone a rigid body rotation as illustrated below.
Overlapping of chain A (grey) with chain B (red) shows that the three helices that normally form the top of the peptide binding site have rotated away from the conserved structural base in chain B, opening up the peptide binding site. This structural change implies that the 14-3-3 molecules do not interact in a rigid way with their target proteins but actively take part in the process changing their conformation as they go from the unbound to the bound state. A schematic picture of the mechanism is illustrated below.

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