2020
Structural properties of target binding by profilaggrin A and B domains and other S100 fused-type calcium-binding proteins
Hinbest AJ, Kim SR, Eldirany SA, Lomakin IB, Watson J, Ho M, Bunick CG. Structural properties of target binding by profilaggrin A and B domains and other S100 fused-type calcium-binding proteins. Journal Of Dermatological Science 2020, 100: 39-49. PMID: 32893105, PMCID: PMC7752840, DOI: 10.1016/j.jdermsci.2020.08.009.Peer-Reviewed Original ResearchAmino Acid SequenceAnnexin A2Binding SitesCrystallography, X-RayFilaggrin ProteinsHumansHydrophobic and Hydrophilic InteractionsIntermediate Filament ProteinsIntermediate FilamentsKeratinocytesKeratinsMolecular Docking SimulationMutationProtein BindingProtein Conformation, alpha-HelicalProtein DomainsProtein PrecursorsRecombinant ProteinsS100 Proteins
2015
Crystal Structure of Human Profilaggrin S100 Domain and Identification of Target Proteins Annexin II, Stratifin, and HSP27
Bunick CG, Presland RB, Lawrence OT, Pearton DJ, Milstone LM, Steitz TA. Crystal Structure of Human Profilaggrin S100 Domain and Identification of Target Proteins Annexin II, Stratifin, and HSP27. Journal Of Investigative Dermatology 2015, 135: 1801-1809. PMID: 25760235, PMCID: PMC4466033, DOI: 10.1038/jid.2015.102.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAnnexin A2Biomarkers, TumorCells, CulturedCrystallizationEpidermal CellsEpidermisExoribonucleasesFilaggrin ProteinsHSP27 Heat-Shock ProteinsHumansIntermediate Filament ProteinsKeratinocytesProtein BindingProtein TransportS100 ProteinsSensitivity and SpecificitySpectrometry, FluorescenceConceptsÅ resolution crystal structureProtein-protein interactionsHuman profilaggrinCalcium-binding domainKeratinocyte terminal differentiationMolecular functionsProtein interactionsTerminal domainShock protein 27Cell envelopeIdentification of targetsN-terminusMolecular approachesTerminal differentiationNormal epidermal barrierHydrophobic pocketSpecific functionsAnnexin IIStable dimerMolecular interfaceProtein 27Proteolytic productsProfilaggrinProteinCrystal structure
2006
Biochemical and Structural Domain Analysis of Xeroderma Pigmentosum Complementation Group C Protein †
Bunick CG, Miller MR, Fuller BE, Fanning E, Chazin WJ. Biochemical and Structural Domain Analysis of Xeroderma Pigmentosum Complementation Group C Protein †. Biochemistry 2006, 45: 14965-14979. PMID: 17154534, PMCID: PMC2579963, DOI: 10.1021/bi061370o.Peer-Reviewed Original ResearchConceptsXPC functionXeroderma pigmentosum complementation group C proteinFirst functional roleComplementation group C proteinFunctional roleProtease protection assaysStructural domain analysesFull-length proteinXeroderma pigmentosum (XP) diseaseLimited proteolysis experimentsN-terminal portionMultidomain proteinsGlobal genomeMutational defectsProtein interactionsAberrant DNAC-terminal fragmentMolecular basisExcision repairProteolysis experimentsBiochemical characterizationC proteinSequence analysisStructural domainsProtection assays