2016
Crystal Structure and Substrate Specificity of PTPN12
Li H, Yang F, Liu C, Xiao P, Xu Y, Liang Z, Liu C, Wang H, Wang W, Zheng W, Zhang W, Ma X, He D, Song X, Cui F, Xu Z, Yi F, Sun J, Yu X. Crystal Structure and Substrate Specificity of PTPN12. Cell Reports 2016, 15: 1345-1358. PMID: 27134172, DOI: 10.1016/j.celrep.2016.04.016.Peer-Reviewed Original ResearchConceptsSubstrate specificityPhosphorylation sitesStructurally plastic regionCdk2 phosphorylation sitesDesign specific inhibitorsSurface loopsCharged residuesMolecular basisTumor suppressorPTPN12Physiological processesBinding pocketSpecific inhibitorsCrystallographic studiesResiduesStructural featuresDesphosphorylationSubstrateCDK2SuppressorCrystal structureSites
1998
Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*
Zhang Z, Devarajan P, Dorfman A, Morrow J. Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*. Journal Of Biological Chemistry 1998, 273: 18681-18684. PMID: 9668035, DOI: 10.1074/jbc.273.30.18681.Peer-Reviewed Original ResearchConceptsK-ATPaseUbiquitous membrane proteinsSecond cytoplasmic domainSpecific macromolecular interactionsMadin-Darby canine kidney cellsAlpha-NACanine kidney cellsCytoplasmic domainThree-dimensional structureMembrane proteinsGlutathione S-transferasePlasma membraneRegulatory proteinsAnkyrinAmino acids bindFusion proteinResidues 142Trisphosphate receptorVectorial transportSurface loopsMacromolecular interactionsMultiple ankyrinHydrophilic faceS-transferaseFusion peptide
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