Identification of the Binding Site for Acidic Phospholipids on the PH Domain of Dynamin: Implications for Stimulation of GTPase Activity
Zheng J, Cahill S, Lemmon M, Fushman D, Schlessinger J, Cowburn D. Identification of the Binding Site for Acidic Phospholipids on the PH Domain of Dynamin: Implications for Stimulation of GTPase Activity. Journal Of Molecular Biology 1996, 255: 14-21. PMID: 8568861, DOI: 10.1006/jmbi.1996.0002.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBlood ProteinsDynaminsGTP PhosphohydrolasesHumansKineticsMagnetic Resonance SpectroscopyModels, MolecularPhosphatidic AcidsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphoproteinsProtein ConformationSequence Homology, Amino AcidSpectrometry, FluorescenceConceptsDynamin PH domainPH domainMembrane associationGTPase activityGuanine nucleotide exchange factorsNucleotide exchange factorsPleckstrin homology domainAcidic phospholipidsBinding of phospholipidsHomology domainExchange factorHuman dynaminGTP hydrolysisDynaminLipid head groupsLigand interactionsGTPaseBinding sitesPhosphatidylinositolSpecific sitesProteinPhospholipidsRelative affinityBindingDomain