14-3-3 protein: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
PRS are homo- and heterodimers containing <scene name='59/590827/Cv/5'>9 antiparallel α-helices</scene>. <scene name='59/590827/Cv/ | 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/7'>Five residues (in PRS-σ and PRS-ζ) are involved in ligand binding</scene>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:14, 27 October 2015
Function14-3-3 proteins (PRS) are conserved regulatory proteins which bind to a multitude of signaling proteins like kinases phosphatases and transmembrane receptors. The name 14-3-3 derives from their elution pattern via chromatography. DiseaseElevated levels of PRS are found in patients with Creutzfeld-Jakob disease (CJD). PRS are associated with Parkinson Disease (PD) and with Alzheimer Disease (AD) based on their localization and their binding to PD and AD-associated proteins. RelevancePRS are tested as biomarkers for CJD, PD and AD. Structural highlightsPRS are homo- and heterodimers containing . (3 helices of chain A are in red and 3 helices of chain B are in magenta). . |
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