2017
Structural insights into POT1-TPP1 interaction and POT1 C-terminal mutations in human cancer
Chen C, Gu P, Wu J, Chen X, Niu S, Sun H, Wu L, Li N, Peng J, Shi S, Fan C, Huang M, Wong CC, Gong Q, Kumar-Sinha C, Zhang R, Pusztai L, Rai R, Chang S, Lei M. Structural insights into POT1-TPP1 interaction and POT1 C-terminal mutations in human cancer. Nature Communications 2017, 8: 14929. PMID: 28393832, PMCID: PMC5394241, DOI: 10.1038/ncomms14929.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsConserved SequenceDNA DamageDNA Mutational AnalysisDNA RepairGenomic InstabilityHumansMiceModels, MolecularMolecular ChaperonesMutationNeoplasmsPhosphoproteinsProstaglandin-E SynthasesProtein BindingProtein Structure, SecondaryScattering, Small AngleShelterin ComplexStructure-Activity RelationshipTelomere-Binding ProteinsX-Ray DiffractionConceptsTelomerase-mediated telomere extensionHuman cancersDNA damage responseC-terminal mutationsOB foldsHuman POT1Chromosome endsGenome instabilityPOT1-TPP1Telomere extensionDamage responseStable heterodimerA-NHEJStructural insightsC-terminusInappropriate repairTPP1POT1Heart-shaped structureMissense mutationsTerminal portionMutationsDomainMutantsTelomeres
2005
Evolutionary Trace-based Peptides Identify a Novel Asymmetric Interaction That Mediates Oligomerization in Nuclear Receptors*
Gu P, Morgan DH, Sattar M, Xu X, Wagner R, Raviscioni M, Lichtarge O, Cooney AJ. Evolutionary Trace-based Peptides Identify a Novel Asymmetric Interaction That Mediates Oligomerization in Nuclear Receptors*. Journal Of Biological Chemistry 2005, 280: 31818-31829. PMID: 15994320, DOI: 10.1074/jbc.m501924200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAmino Acid SequenceCell LineDimerizationDNA-Binding ProteinsEvolution, MolecularGenes, ReporterMolecular Sequence DataNuclear Receptor Subfamily 6, Group A, Member 1PeptidesPoint MutationProtein Structure, SecondaryProtein Structure, TertiaryReceptor Cross-TalkReceptors, Cytoplasmic and NuclearReceptors, Retinoic AcidResponse ElementsConceptsGerm cell nuclear factorEvolutionary trace analysisNuclear receptorsKey functional sitesOrphan nuclear receptorDR0 elementsGCNF bindsComplex formationEssential genesEvolutionary traceMolecular basisOligomerization propertiesHelix 3Heterotypic interactionsTargeted mutationsLarge complexesNovel helixFunctional sitesHelix 11HomodimerNuclear factorDimerizationOligomerizationHelixMutations