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Article: P-loop flexibility in Na+ channel pores revealed by single- and double- cysteine replacements

TitleP-loop flexibility in Na+ channel pores revealed by single- and double- cysteine replacements
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1997
PublisherRockefeller University Press. The Journal's web site is located at www.jgp.org/
Citation
Journal Of General Physiology, 1997, v. 110 n. 1, p. 59-72 How to Cite?
AbstractReplacement of individual P-loop residues with cysteines in rat skeletal muscle Na+ channels (SkMI) caused an increased sensitivity to current blockade by Cd2+ thus allowing detection of residues lining the pore. Simultaneous replacement of two residues in distinct P-loops created channels with enhanced and reduced sensitivity to Cd2+ block relative to the individual single mutants, suggesting coordinated Cd2+ binding and cross- linking by the inserted sulfhydryl pairs. Double-mutant channels with reduced sensitivity to Cd2+ block showed enhanced sensitivity after the application of sulfhydryl reducing agents. These results allow identification of residue pairs capable of approaching one another to within less than 3.5 Å. We often observed that multiple consecutive adjacent residues in one P-loop could coordinately bind Cd2+ with a single residue in another P-loop. These results suggest that, on the time-scale of Cd2+ binding to mutant Na+ channels, P-loops show a high degree of flexibility.
Persistent Identifierhttp://hdl.handle.net/10722/91465
ISSN
2015 Impact Factor: 4.511
2015 SCImago Journal Rankings: 3.061
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTsushima, RGen_HK
dc.contributor.authorLi, RAen_HK
dc.contributor.authorBackx, PHen_HK
dc.date.accessioned2010-09-17T10:19:51Z-
dc.date.available2010-09-17T10:19:51Z-
dc.date.issued1997en_HK
dc.identifier.citationJournal Of General Physiology, 1997, v. 110 n. 1, p. 59-72en_HK
dc.identifier.issn0022-1295en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91465-
dc.description.abstractReplacement of individual P-loop residues with cysteines in rat skeletal muscle Na+ channels (SkMI) caused an increased sensitivity to current blockade by Cd2+ thus allowing detection of residues lining the pore. Simultaneous replacement of two residues in distinct P-loops created channels with enhanced and reduced sensitivity to Cd2+ block relative to the individual single mutants, suggesting coordinated Cd2+ binding and cross- linking by the inserted sulfhydryl pairs. Double-mutant channels with reduced sensitivity to Cd2+ block showed enhanced sensitivity after the application of sulfhydryl reducing agents. These results allow identification of residue pairs capable of approaching one another to within less than 3.5 Å. We often observed that multiple consecutive adjacent residues in one P-loop could coordinately bind Cd2+ with a single residue in another P-loop. These results suggest that, on the time-scale of Cd2+ binding to mutant Na+ channels, P-loops show a high degree of flexibility.en_HK
dc.languageengen_HK
dc.publisherRockefeller University Press. The Journal's web site is located at www.jgp.org/en_HK
dc.relation.ispartofJournal of General Physiologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleP-loop flexibility in Na+ channel pores revealed by single- and double- cysteine replacementsen_HK
dc.typeArticleen_HK
dc.identifier.emailLi, RA:ronaldli@HKUCC.hku.hken_HK
dc.identifier.authorityLi, RA=rp1352en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1085/jgp.110.1.59en_HK
dc.identifier.pmid9234171-
dc.identifier.scopuseid_2-s2.0-0030753096en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030753096&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume110en_HK
dc.identifier.issue1en_HK
dc.identifier.spage59en_HK
dc.identifier.epage72en_HK
dc.identifier.isiWOS:A1997XJ48000006-
dc.publisher.placeUnited Statesen_HK

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