2010
Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity
Petri ET, Ćelić A, Kennedy SD, Ehrlich BE, Boggon TJ, Hodsdon ME. Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 9176-9181. PMID: 20439752, PMCID: PMC2889120, DOI: 10.1073/pnas.0912295107.Peer-Reviewed Original ResearchConceptsEF-hand domainPolycystin-2Dependent protein interactionsTerminal cytoplasmic tailSequence conservation analysisPC2 channel activityChannel activityDependent conformational changesMechanism of regulationEF-hand motifsHLH motifHelix motifCytoplasmic tailCoil domainProtein interactionsConservation analysisDependent regulationNMR structureSensitive regulationConformational changesSensitive regulatorFunctional regionsFlexible linkerPermeable channelsPC2 activity
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
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