2015
Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site
Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA. Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site. Structure 2015, 23: 352-363. PMID: 25620000, PMCID: PMC4319572, DOI: 10.1016/j.str.2014.12.009.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCrystallography, X-RayGreen Fluorescent ProteinsGTPase-Activating ProteinsHeLa CellsHumansInositol PhosphatesModels, MolecularMolecular Sequence DataProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSpecies SpecificityConceptsF-BAR domainLipid-binding specificityMembrane-binding propertiesNumerous functional studiesPhosphate binding siteUnappreciated determinantF-BARDomain bindsCell signalingCurved membranesMembrane interactionsFunctional studiesRgd1pBinding sitesX-ray crystal structureInositol phosphatesDomain structureDomainHof1pPhospholipidsRhoGAPCytokinesisEndocytosisPhosphoinositideSignaling
2009
Mechanistic Insights into Membrane Remodeling Through BAR‐Domain Proteins
Frost A, Mim C, Perera R, Spasov K, Egelman E, De Camilli P, Unger V. Mechanistic Insights into Membrane Remodeling Through BAR‐Domain Proteins. The FASEB Journal 2009, 23: 82.2-82.2. DOI: 10.1096/fasebj.23.1_supplement.82.2.Peer-Reviewed Original ResearchF-BAR domainBAR domain proteinsMembrane-bound stateDifferent molecular surfacesMembrane remodelingCellular physiologyMembrane curvatureElectron cryomicroscopyMechanistic insightsCooperative assemblyConstituent membranesProteinStructural informationMolecular surfaceFunctional stateMembraneDomainSubtle changesCryomicroscopyBilayer substratePhysiologyStructural modelAssemblyRemodelingCells
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