2009
Contribution of individual histidines to the global stability of human prolactin
Keeler C, Tettamanzi MC, Meshack S, Hodsdon ME. Contribution of individual histidines to the global stability of human prolactin. Protein Science 2009, 18: 909-920. PMID: 19384991, PMCID: PMC2771294, DOI: 10.1002/pro.100.Peer-Reviewed Original ResearchConceptsIndividual histidineClosest evolutionary cousinsEvolutionary roleDouble mutant cyclesHomologous residuesEvolutionary cousinsNearby histidineExtracellular domainNative proteinTertiary structureStability of hGHNative stateMutant cyclesHuman growth hormoneHistidineStructural interactionsHuman prolactinResiduesPolypeptide hormonesPhysiologic pH rangeFunctional propertiesStructural locationAffinityProteinMutations
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