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Probing the channel-bound shaker B inactivating peptide by stereoisomeric substitution at a strategic tyrosine residue

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dc.contributor.authorEncinar Hidalgo, José Antonio
dc.contributor.authorFernández Carvajal, Asia María
dc.contributor.authorPoveda Larrosa, José Antonio
dc.contributor.authorMolina Gallego, María Luisa
dc.contributor.authorAlbar, J.P.
dc.contributor.authorGavilanes Franco, Francisco
dc.contributor.authorGonzález Ros, José Manuel
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2024-07-03T10:42:26Z
dc.date.available2024-07-03T10:42:26Z
dc.date.issued2003-07-01
dc.description© 2003 American Chemical Society. This document is the Published version of a Published Work that appeared in final form in Biochemistry. To access the final edited and published work see https://doi.org/10.1021/bi0343121
dc.description.abstractA synthetic peptide patterned after the sequence of the inactivating ball domain of the Shaker B K+ channel, the ShB peptide, fully restores fast inactivation in the deletion Shaker BΔ6−46 K+ channel, which lacks the constitutive ball domains. On the contrary, a similar peptide in which tyrosine 8 is substituted by the secondary structure-disrupting d-tyrosine stereoisomer does not. This suggests that the stereoisomeric substitution prevents the peptide from adopting a structured conformation when bound to the channel during inactivation. Moreover, characteristic in vitro features of the wild-type ShB peptide such as the marked propensity to adopt an intramolecular β-hairpin structure when challenged by anionic phospholipid vesicles, a model target mimicking features of the inactivation site in the channel protein, or to insert into their hydrophobic bilayers, are lost in the d-tyrosine-containing peptide, whose behavior is practically identical to that of noninactivating peptide mutants. In the absence of high resolution crystallographic data on the inactivated channel/peptide complex, these latter findings suggest that the structured conformation required for the peptide to promote channel inactivation, as referred to above, is likely to be β-hairpin.es
dc.formatapplication/pdfes
dc.format.extent6es
dc.identifier.citationBiochemistry 2003, 42, 29, 8879–8884
dc.identifier.doihttps://doi.org/10.1021/bi0343121
dc.identifier.issnPrint: 0006-2960
dc.identifier.issnElectronic: 1520-4995
dc.identifier.urihttp://hdl.handle.net/10201/142831
dc.languageenges
dc.publisherAmerican Chemical Society
dc.relationPartly supported by grants from the Spanish DGI BFI2002-03410 and BMC2000-0545es
dc.relation.publisherversionhttps://pubs.acs.org/doi/10.1021/bi0343121
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectGeneticses
dc.subjectMonomerses
dc.subjectPeptides and proteinses
dc.subjectPotassiumes
dc.subjectVesicleses
dc.titleProbing the channel-bound shaker B inactivating peptide by stereoisomeric substitution at a strategic tyrosine residuees
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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