A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase
Goldstein D, Kulke R, Dimaio D, Schlegel R. A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase. Journal Of Virology 1992, 66: 405-413. PMID: 1370089, PMCID: PMC238300, DOI: 10.1128/jvi.66.1.405-413.1992.Peer-Reviewed Original ResearchConceptsK proteinGrowth factor receptorE5 oncoproteinGlutamine residuesRandom hydrophobic sequencesSpecific amino acid residuesMembrane-associated domainMajor transforming proteinK protein componentCarboxyl-terminal domainEndoplasmic reticulum membraneFactor receptorBovine papillomavirus type 1Colony-stimulating factor 1 receptorTransformation-defective mutantsAmino acid residuesPotential binding sitesPlatelet-derived growth factor receptorAmino acid substitutionsPapillomavirus type 1Hydrophilic amino acidsE5 dimerE5 mutantsFactor 1 receptorProtein complexes