Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain
Uellner R, Zvelebil M, Hopkins J, Jones J, MacDougall L, Morgan B, Podack E, Waterfield M, Griffiths G. Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain. The EMBO Journal 1997, 16: 7287-7296. PMID: 9405358, PMCID: PMC1170329, DOI: 10.1093/emboj/16.24.7287.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCytotoxicity, ImmunologicGlycosylationHexosaminidasesHumansIsoenzymesKiller Cells, NaturalLiposomesLymphocyte ActivationMembrane GlycoproteinsModels, MolecularMolecular Sequence DataPerforinPhospholipase C deltaPhospholipidsPore Forming Cytotoxic ProteinsProtein ConformationProtein Processing, Post-TranslationalRatsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTransfectionType C PhospholipasesConceptsC2 domainPro-pieceProteolytic cleavagePlasma membrane of target cellsBind phospholipid membranesMembrane of target cellsCalcium-dependent mannerSecreted proteinsIntracellular transportC-terminusPhospholipid membranesNK cell line YTPlasma membraneCleaved formInactive precursorAcidic compartmentsIncreased lytic activityConcanamycin AActive formLytic activityKilling assayE-64CleavageEpitope mappingPore formation
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