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dc.contributor.authorSrinivasan, KN
dc.contributor.authorNirthanan, S
dc.contributor.authorSasaki, T
dc.contributor.authorSato, K
dc.contributor.authorCheng, B
dc.contributor.authorGwee, MCE
dc.contributor.authorKini, RM
dc.contributor.authorGopalakrishnakone, P
dc.date.accessioned2009-07-09
dc.date.accessioned2014-04-10T05:15:33Z
dc.date.accessioned2017-03-02T00:12:01Z
dc.date.available2017-03-02T00:12:01Z
dc.date.issued2001
dc.date.modified2014-04-10T05:15:33Z
dc.identifier.issn0014-5793
dc.identifier.doi10.1016/S0014-5793(01)02342-0
dc.identifier.urihttp://hdl.handle.net/10072/58202
dc.description.abstractAlpha-toxins from scorpion venoms prolong the action potential of excitable cells by blocking sodium channel inactivation. We have purified bukatoxin, an alpha-toxin from scorpion (Buthus martensi Karsch) venom, to homogeneity. Bukatoxin produced marked relaxant responses in the carbachol-precontracted rat anococcygeus muscle (ACM), which were mediated through the L-arginine-nitric oxide synthase-nitric oxide pathway, consequent to a neuronal release of nitric oxide. Based on the presence of proline residues in the flanking segments of protein-protein interaction sites, we predicted the site between (52)PP(56) to be the potential interaction site of bukatoxin. A homology model of bukatoxin indicated the presence of this site on the surface. Buka11, a synthetic peptide designed based on this predicted site, produced a concentration-dependent nitric oxide-mediated relaxant response in ACM. Using alanine-substituted peptides, we have shown the importance (53)DKV(55) flanked by proline residues in the functional site of bukatoxin.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.publisherElsevier B.V.
dc.publisher.placeAmsterdam, The Netherlands
dc.relation.ispartofpagefrom145
dc.relation.ispartofpageto149
dc.relation.ispartofissue3
dc.relation.ispartofjournalFEBS Letters
dc.relation.ispartofvolume494
dc.subject.fieldofresearchBasic Pharmacology
dc.subject.fieldofresearchBioinformatics
dc.subject.fieldofresearchAutonomic Nervous System
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchEvolutionary Biology
dc.subject.fieldofresearchcode111501
dc.subject.fieldofresearchcode060102
dc.subject.fieldofresearchcode110901
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0601
dc.subject.fieldofresearchcode0603
dc.titleFunctional site of bukatoxin, an alpha-type sodium channel neurotoxin from the Chinese scorpion (Buthus martensi Karsch) venom: probable role of the (52)PDKVP(56) loop.
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codec1x
gro.facultyGriffith Health Faculty
gro.date.issued2001
gro.hasfulltextNo Full Text
gro.griffith.authorNirthanan, Niru


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