Publication: Probing the channel-bound shaker B inactivating peptide by stereoisomeric substitution at a strategic tyrosine residue
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Date
2003-07-01
Authors
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
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Publisher
American Chemical Society
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DOI
https://doi.org/10.1021/bi0343121
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info:eu-repo/semantics/article
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
Abstract
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.
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Citation
Biochemistry 2003, 42, 29, 8879–8884
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