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
2004
Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †
Scheuermann TH, Keeler C, Hodsdon ME. Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †. Biochemistry 2004, 43: 12198-12209. PMID: 15379558, DOI: 10.1021/bi0492556.Peer-Reviewed Original ResearchConceptsNMR chemical shift mapping experimentsChemical shift mapping experimentsNative structureS-adenosylmethionineProteasomal-dependent pathwayCatalytic mechanismProtein backboneIntracellular degradationIndirect conformational changesS-adenosylmethionine analogPresence of sinefunginBacterial orthologuesChemical shift changesProtein backbone dynamicsPseudomonas syringaeSubstrate recognitionProtein sequencesSAM analoguesConformational changesNMR spectroscopyBackbone dynamicsMapping experimentsBackbone mobilitySinefunginNMR relaxation