2009
A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism
Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P. A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism. The EMBO Journal 2009, 28: 1831-1842. PMID: 19536138, PMCID: PMC2711190, DOI: 10.1038/emboj.2009.155.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesClathrinCoated VesiclesEndocytosisHeLa CellsHumansModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositolsPhospholipidsPhosphoric Monoester HydrolasesProtein ConformationProtein Structure, TertiaryRatsSequence AlignmentConceptsPH domainNH2-terminal portionEndocytic clathrin-coated pitsClathrin-binding siteClathrin-coated pitsNMR structure determinationNH2-terminal regionCOOH-terminal regionClathrin-box motifsMembrane traffickingEvolutionary pressureSimilar proteinsINPP5BOCRLSpecialized functionsSequence dissimilarityLowe syndromePhosphoinositide metabolismDent's diseaseHeavy chainMutationsRecruitment efficiencyStructure determinationMetabolismDomain
2008
Analysis of Site-Specific Histidine Protonation in Human Prolactin ,
Tettamanzi MC, Keeler C, Meshack S, Hodsdon ME. Analysis of Site-Specific Histidine Protonation in Human Prolactin ,. Biochemistry 2008, 47: 8638-8647. PMID: 18652486, PMCID: PMC2766358, DOI: 10.1021/bi800444t.Peer-Reviewed Original ResearchConceptsPH-dependent regulationSite-directed mutagenesisExtracellular domainHistidine residuesHistidine protonationStatistical supportHPRL receptorFunctional propertiesHuman prolactinProtein surfaceBiophysical mechanismsBiophysical originApparent midpointEquilibrium dissociation constantsHistidineResiduesProtein hormonesDetailed understandingCooperativity constantsSurprising numberDissociation rateMutagenesisDissociation constantsProteinNMR spectroscopy
2003
Tertiary Structure of Thiopurine Methyltransferase from Pseudomonas syringae, a Bacterial Orthologue of a Polymorphic, Drug-metabolizing Enzyme
Scheuermann TH, Lolis E, Hodsdon ME. Tertiary Structure of Thiopurine Methyltransferase from Pseudomonas syringae, a Bacterial Orthologue of a Polymorphic, Drug-metabolizing Enzyme. Journal Of Molecular Biology 2003, 333: 573-585. PMID: 14556746, DOI: 10.1016/j.jmb.2003.08.039.Peer-Reviewed Original ResearchConceptsTertiary structureBacterial orthologuesPseudomonas syringaeConsensus topologyProteasomal-dependent pathwayEnzymatic activitySAM-dependent methyltransferasesUnstructured N-terminusSequence similarityThree-dimensional structureShares 45Dependent transmethylationProtein sequencesN-terminusHuman enzymePolymorphic proteinsBiochemical studiesS-adenosylmethionineOrthologuesSyringaeMethyltransferaseTissue enzymatic activityThiopurine methyltransferaseIntracellular conversionMultiple insertions