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 determinationMetabolismDomainContribution 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