2010
Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*
Li X, Zhang R, Zhang H, He Y, Ji W, Min W, Boggon TJ. Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*. Journal Of Biological Chemistry 2010, 285: 24099-24107. PMID: 20489202, PMCID: PMC2911348, DOI: 10.1074/jbc.m110.128470.Peer-Reviewed Original ResearchMeSH KeywordsApoptosis Regulatory ProteinsBinding, CompetitiveBrainCrystallography, X-RayDimerizationHemangioma, Cavernous, Central Nervous SystemHumansKineticsMembrane ProteinsMolecular ConformationMutationPaxillinProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene ProteinsConceptsN-terminal dimerization domainPaxillin LD motifsCerebral cavernous malformationsAlpha-helical proteinsLD motifsCCM complexHomology domainFocal adhesionsDimerization domainMolecular basisHydrophobic pocketHuman populationCCM3 mutationsMutationsCCM3Crystal structureVascular integrityCCM2DomainPaxillinProteinMotifCCM1InteractionCells
2007
Structural and Functional Characterization of the Human Protein Kinase ASK1
Bunkoczi G, Salah E, Filippakopoulos P, Fedorov O, Müller S, Sobott F, Parker SA, Zhang H, Min W, Turk BE, Knapp S. Structural and Functional Characterization of the Human Protein Kinase ASK1. Structure 2007, 15: 1215-1226. PMID: 17937911, PMCID: PMC2100151, DOI: 10.1016/j.str.2007.08.011.Peer-Reviewed Original ResearchConceptsApoptosis signal-regulating kinase 1Autophosphorylation sitesSignal-regulated kinases 1ASK1 kinase activityVitro autophosphorylation sitesAnalytical ultracentrifugationHigh-resolution structuresATP-mimetic inhibitorSite-directed mutantsReporter gene assayPhosphorylation motifsPhosphorylation sitesCatalytic domainFunctional characterizationKinase activityRegulatory mechanismsKinase 1Tight dimerMimetic inhibitorsGene assayEssential roleSelective inhibitorTail fashionCrystallographic analysisMass spectrometry