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Article: Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BK Ca channel

TitleBlocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BK Ca channel
Authors
Issue Date2005
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistry
Citation
Biochemistry, 2005, v. 44 n. 30, p. 10145-10152 How to Cite?
AbstractCysteine-rich secretory proteins (CRISPs) are widespread in snake venoms. Some members of these CRISPs recently have been found to block L-type Ca 2+ channels or cyclic nucleotide-gated ion (CNG) channels. Here, natrin purified from Naja atra venom, a member of the CRISP family, can induce a further contractile response in the endothelium-denuded thoracic aorta of mouse which has been contracted by a high-K + solution. Further experiments show it can block the high-conductance calcium-activated potassium (BK ca) channel in a concentration-dependent manner with an IC 50 of 34.4 nM and a Hill coefficient of 1.02, which suggests that only a single natrin molecule is required to bind an ion channel to block BK ca current. The crystal structure of natrin displaying two domains in tandem shows its cysteinerich domain (CRD) has relatively independent flexibility, especially for the C-terminal long loop (loop I) of CRD to participate in the interface of two domains. On the basis of previous studies of CNG channel and L-Ca 2- channel blockers, and the sequence and structural comparison of natrin and stecrisp, the deviation of the vital loop I of CRD is suggested to contribute to different effects of some CRISPs in protein-protein interaction. © 2005 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/91955
ISSN
2015 Impact Factor: 2.876
2015 SCImago Journal Rankings: 1.769
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Jen_HK
dc.contributor.authorShen, Ben_HK
dc.contributor.authorGuo, Men_HK
dc.contributor.authorLou, Xen_HK
dc.contributor.authorDuan, Yen_HK
dc.contributor.authorCheng, XPen_HK
dc.contributor.authorTeng, Men_HK
dc.contributor.authorNiu, Len_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHuang, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.date.accessioned2010-09-17T10:31:36Z-
dc.date.available2010-09-17T10:31:36Z-
dc.date.issued2005en_HK
dc.identifier.citationBiochemistry, 2005, v. 44 n. 30, p. 10145-10152en_HK
dc.identifier.issn0006-2960en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91955-
dc.description.abstractCysteine-rich secretory proteins (CRISPs) are widespread in snake venoms. Some members of these CRISPs recently have been found to block L-type Ca 2+ channels or cyclic nucleotide-gated ion (CNG) channels. Here, natrin purified from Naja atra venom, a member of the CRISP family, can induce a further contractile response in the endothelium-denuded thoracic aorta of mouse which has been contracted by a high-K + solution. Further experiments show it can block the high-conductance calcium-activated potassium (BK ca) channel in a concentration-dependent manner with an IC 50 of 34.4 nM and a Hill coefficient of 1.02, which suggests that only a single natrin molecule is required to bind an ion channel to block BK ca current. The crystal structure of natrin displaying two domains in tandem shows its cysteinerich domain (CRD) has relatively independent flexibility, especially for the C-terminal long loop (loop I) of CRD to participate in the interface of two domains. On the basis of previous studies of CNG channel and L-Ca 2- channel blockers, and the sequence and structural comparison of natrin and stecrisp, the deviation of the vital loop I of CRD is suggested to contribute to different effects of some CRISPs in protein-protein interaction. © 2005 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistryen_HK
dc.relation.ispartofBiochemistryen_HK
dc.titleBlocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BK Ca channelen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/bi050614men_HK
dc.identifier.pmid16042391-
dc.identifier.scopuseid_2-s2.0-23044468262en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-23044468262&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume44en_HK
dc.identifier.issue30en_HK
dc.identifier.spage10145en_HK
dc.identifier.epage10152en_HK
dc.identifier.isiWOS:000230879900019-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWang, J=36078440500en_HK
dc.identifier.scopusauthoridShen, B=8958686600en_HK
dc.identifier.scopusauthoridGuo, M=34569788700en_HK
dc.identifier.scopusauthoridLou, X=16024965700en_HK
dc.identifier.scopusauthoridDuan, Y=36857720100en_HK
dc.identifier.scopusauthoridCheng, XP=34973976200en_HK
dc.identifier.scopusauthoridTeng, M=7101891754en_HK
dc.identifier.scopusauthoridNiu, L=7101760477en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHuang, Q=7403634448en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK

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