2014
Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry
Sriswasdi S, Harper SL, Tang HY, Gallagher PG, Speicher DW. Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 1801-1806. PMID: 24453214, PMCID: PMC3918770, DOI: 10.1073/pnas.1317620111.Peer-Reviewed Original ResearchMeSH KeywordsBiophysical PhenomenaMass SpectrometryMutant ProteinsProtein MultimerizationProtein Structure, QuaternarySpectrinConceptsMass spectrometryConformational changesStructural mass spectrometryLarge conformational rearrangementsCell membraneMembrane integrityMass spectrometry characterizationRed cell spectrinUnidentified mechanistic insightCell membrane integrityProtein complexesMacromolecular complexesDiverse functionsCell shapeBiological processesFlexible proteinsConformational rearrangementsDimer-tetramer equilibriumRed cell membraneOpen dimersCell typesΑ-spectrinKey mechanistic roleTetramerization siteBiophysical data
2013
The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation
Harper SL, Sriswasdi S, Tang HY, Gaetani M, Gallagher PG, Speicher DW. The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. Blood 2013, 122: 3045-3053. PMID: 23974198, PMCID: PMC3811177, DOI: 10.1182/blood-2013-02-487702.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCross-Linking ReagentsElliptocytosis, HereditaryErythrocyte MembraneHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSpectrinConceptsHereditary elliptocytosisMembrane destabilizationLarge conformational rearrangementsGel filtration analysisMembrane proteinsTetramer assemblyHereditary pyropoikilocytosisBiophysical analysisCommon hereditary elliptocytosisConformational rearrangementsDimer conformationHelical contentTetramerization siteFiltration analysisSpectrin tetramersNovel mechanismUnknown mechanismMutationsBinding assaysSpectrinChemical crosslinkingErythrocyte shapeTetramerErythrocyte membranesMembrane
2010
A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin [S] *
Li D, Harper SL, Tang HY, Maksimova Y, Gallagher PG, Speicher DW. A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin [S] *. Journal Of Biological Chemistry 2010, 285: 29535-29545. PMID: 20610390, PMCID: PMC2937985, DOI: 10.1074/jbc.m110.145573.Peer-Reviewed Original ResearchConceptsHelix faceRed cell membrane stabilityHomology modelingNon-homologous tailsCell membrane stabilityC-terminal tailWild-type bindingMedium-resolution structureSubtle conformational changesTetramer complexSpectrin tetramer formationChemical Cross-LinkingMembrane skeletonRecombinant domainsTetramer formationA Fused α-β “Mini-spectrin” Mimics the Intact Erythrocyte Spectrin Head-to-head Tetramer*
Harper SL, Li D, Maksimova Y, Gallagher PG, Speicher DW. A Fused α-β “Mini-spectrin” Mimics the Intact Erythrocyte Spectrin Head-to-head Tetramer*. Journal Of Biological Chemistry 2010, 285: 11003-11012. PMID: 20139081, PMCID: PMC2856305, DOI: 10.1074/jbc.m109.083048.Peer-Reviewed Original ResearchConceptsN-terminal regionFull-length dimerC-terminal regionRed cell membrane integrityGel filtration analysisLateral associationCell membrane integrityOligomeric stateFusion proteinAlpha-spectrinTetramer formationBeta subunitC-terminalN-terminalConformational statesFunctional studiesFiltration analysisMembrane integritySpectrin heterodimersTerminal peptidesDimer interactionsDistinct groupsSpectrinSpectrin dimersProtein