2wh0 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The phosphoserine/threonine binding protein 14-3-3 stimulates the catalytic activity of protein kinase C-epsilon (PKCepsilon) by engaging two tandem phosphoserine-containing motifs located between the PKCepsilon regulatory and catalytic domains (V3 region). Interaction between 14-3-3 and this region of PKCepsilon is essential for the completion of cytokinesis. Here, we report the crystal structure of 14-3-3zeta bound to a synthetic diphosphorylated PKCepsilon V3 region revealing how a consensus 14-3-3 site and a divergent 14-3-3 site cooperate to bind to 14-3-3 and so activate PKCepsilon. Thermodynamic data show a markedly enhanced binding affinity for two-site phosphopeptides over single-site 14-3-3 binding motifs and identifies Ser 368 as a gatekeeper phosphorylation site in this physiologically relevant 14-3-3 ligand. This dual-site intra-chain recognition has implications for other 14-3-3 targets, which seem to have only a single 14-3-3 motif, as other lower affinity and cryptic 14-3-3 gatekeeper sites might exist.
Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon.,Kostelecky B, Saurin AT, Purkiss A, Parker PJ, McDonald NQ EMBO Rep. 2009 Sep;10(9):983-9. Epub 2009 Aug 7. PMID:19662078[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Kostelecky B, Saurin AT, Purkiss A, Parker PJ, McDonald NQ. Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon. EMBO Rep. 2009 Sep;10(9):983-9. Epub 2009 Aug 7. PMID:19662078 doi:10.1038/embor.2009.150
