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https://doi.org/10.1021/bi0343121
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Título: | Probing the channel-bound shaker B inactivating peptide by stereoisomeric substitution at a strategic tyrosine residue |
Fecha de publicación: | 1-jul-2003 |
Editorial: | American Chemical Society |
Cita bibliográfica: | Biochemistry 2003, 42, 29, 8879–8884 |
ISSN: | Print: 0006-2960 Electronic: 1520-4995 |
Palabras clave: | Genetics Monomers Peptides and proteins Potassium Vesicles |
Resumen: | A 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. |
Autor/es principal/es: | Encinar Hidalgo, José Antonio Fernández Carvajal, Asia María Poveda Larrosa, José Antonio Molina Gallego, María Luisa Albar, J.P. Gavilanes Franco, Francisco González Ros, José Manuel |
Facultad/Departamentos/Servicios: | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Bioquímica y Biología Molecular "B" e Inmunología |
Versión del editor: | https://pubs.acs.org/doi/10.1021/bi0343121 |
URI: | http://hdl.handle.net/10201/142831 |
DOI: | https://doi.org/10.1021/bi0343121 |
Tipo de documento: | info:eu-repo/semantics/article |
Número páginas / Extensión: | 6 |
Derechos: | info:eu-repo/semantics/embargoedAccess |
Descripción: | © 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 |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "B" e Inmunología |
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