14-3-3 protein

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Revision as of 11:19, 16 December 2018

Structure of human 14-3-3 protein ζ with phosphopeptide (yellow) (PDB code 1qja).

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↑ Benzinger A, Popowicz GM, Joy JK, Majumdar S, Holak TA, Hermeking H. The crystal structure of the non-liganded 14-3-3sigma protein: insights into determinants of isoform specific ligand binding and dimerization. Cell Res. 2005 Apr;15(4):219-27. PMID:15857576 doi:10.1038/sj.cr.7290290

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 == Structural highlights ==
-PRS are homo- and heterodimers containing <scene name='59/590827/Cv/5'>9 antiparallel α-helices</scene>. <scene name='59/590827/Cv/12'>Three of the helices form the dimerization domain</scene> (<font color='red'><b>3 helices of chain A are in red</b></font> and <font color='magenta'><b>3 helices of chain B are in magenta</b></font>). <scene name='59/590827/Cv/13'>Five residues (in PRS-σ and PRS-ζ) are involved in ligand binding</scene>.
+PRS are homo- and heterodimers containing <scene name='59/590827/Cv/14'>9 antiparallel α-helices</scene>. <scene name='59/590827/Cv/15'>Three of the helices form the dimerization domain</scene> (<font color='red'><b>3 helices of chain A are in red</b></font> and <font color='magenta'><b>3 helices of chain B are in magenta</b></font>). <scene name='59/590827/Cv/16'>Five residues (in PRS-σ and PRS-ζ) are involved in ligand binding</scene>.
 </StructureSection>