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
2006
Solution structure and backbone dynamics of an N‐terminal ubiquitin‐like domain in the GLUT4‐regulating protein, TUG
Tettamanzi MC, Yu C, Bogan JS, Hodsdon ME. Solution structure and backbone dynamics of an N‐terminal ubiquitin‐like domain in the GLUT4‐regulating protein, TUG. Protein Science 2006, 15: 498-508. PMID: 16501224, PMCID: PMC2249771, DOI: 10.1110/ps.051901806.Peer-Reviewed Original ResearchConceptsN-terminal ubiquitin-like domainUbiquitin-like domainC-terminal diglycine motifPotential protein-protein interaction sitesN-terminal UBL domainAcceptor lysine residuesBackbone dynamicsProtein-protein interactionsProtein-protein interaction sitesSpecific cellular processesUbiquitin-proteasome pathwayLack of conservationProtein modification reactionUBL domainCellular processesDiglycine motifExocytic machineryUbiquitin recognitionAcceptor lysinePlasma membraneMolecular basisInsulin stimulationLysine residuesMembrane vesiclesTertiary structure
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