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Article: Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K + channel inhibitor-like fold

TitleCrystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K + channel inhibitor-like fold
Authors
KeywordsMolecular Sequence Numbers
Issue Date2005
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2005, v. 280 n. 13, p. 12405-12412 How to Cite?
AbstractStecrisp from Trimeresurus stejnegeri snake venom belongs to a family of cysteine-rich secretory proteins (CRISP) that have various functions related to spermegg fusion, innate host defense, and the blockage of ion channels. Here we present the crystal structure of stecrisp refined to 1.6-Å resolution. It shows that stecrisp contains three regions, namely a PR-1 (pathogenesis-related proteins of group1) domain, a hinge, and a cysteine-rich domain (CRD). A conformation of solvent-exposed and -conserved residues (His 60, Glu 75, Glu 96, and His 115) in the PR-1 domain similar to that of their counterparts in homologous structures suggests they may share some molecular mechanism. Three flexible loops of hypervariable sequence surrounding the possible substrate binding site in the PR-1 domain show an evident difference in homologous structures, implying that a great diversity of species- and substrate-specific interactions may be involved in recognition and catalysis. The hinge is fixed by two crossed disulfide bonds formed by four of ten characteristic cysteines in the carboxyl-terminal region and is important for stabilizing the N-terminal PR-1 domain. Spatially separated from the PR-1 domain, CRD possesses a similar fold with two K + channel inhibitors (Bgk and Shk). Several candidates for the possible functional sites of ion channel blocking are located in a solvent-exposed loop in the CRD. The structure of stecrisp will provide a prototypic architecture for a structural and functional exploration of the diverse members of the CRISP family. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/91897
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGuo, Men_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.accessioned2010-09-17T10:29:53Z-
dc.date.available2010-09-17T10:29:53Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2005, v. 280 n. 13, p. 12405-12412en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91897-
dc.description.abstractStecrisp from Trimeresurus stejnegeri snake venom belongs to a family of cysteine-rich secretory proteins (CRISP) that have various functions related to spermegg fusion, innate host defense, and the blockage of ion channels. Here we present the crystal structure of stecrisp refined to 1.6-Å resolution. It shows that stecrisp contains three regions, namely a PR-1 (pathogenesis-related proteins of group1) domain, a hinge, and a cysteine-rich domain (CRD). A conformation of solvent-exposed and -conserved residues (His 60, Glu 75, Glu 96, and His 115) in the PR-1 domain similar to that of their counterparts in homologous structures suggests they may share some molecular mechanism. Three flexible loops of hypervariable sequence surrounding the possible substrate binding site in the PR-1 domain show an evident difference in homologous structures, implying that a great diversity of species- and substrate-specific interactions may be involved in recognition and catalysis. The hinge is fixed by two crossed disulfide bonds formed by four of ten characteristic cysteines in the carboxyl-terminal region and is important for stabilizing the N-terminal PR-1 domain. Spatially separated from the PR-1 domain, CRD possesses a similar fold with two K + channel inhibitors (Bgk and Shk). Several candidates for the possible functional sites of ion channel blocking are located in a solvent-exposed loop in the CRD. The structure of stecrisp will provide a prototypic architecture for a structural and functional exploration of the diverse members of the CRISP family. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.subjectMolecular Sequence Numbersen_HK
dc.titleCrystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K + channel inhibitor-like folden_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.doi10.1074/jbc.M413566200en_HK
dc.identifier.pmid15596436-
dc.identifier.scopuseid_2-s2.0-16844376656en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-16844376656&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume280en_HK
dc.identifier.issue13en_HK
dc.identifier.spage12405en_HK
dc.identifier.epage12412en_HK
dc.identifier.isiWOS:000227922000042-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridGuo, M=34569788700en_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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