Probing the Channel-BoundShakerB Inactivating Peptide by Stereoisomeric Substitution at a Strategic Tyrosine Residue†

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

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 BDelta6-46 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. Thi...

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Tyrosine phosphorylation of the inactivating peptide of the shaker B potassium channel: a structural-functional correlate.

A synthetic peptide patterned after the sequence of the inactivating "ball" domain of the Shaker B K(+) channel restores fast (N-type) inactivation in mutant deletion channels lacking their constitutive ball domains, as well as in K(+) channels that do not normally inactivate. We now report on the effect of phosphorylation at a single tyrosine in position 8 of the inactivating peptide both on i...

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Synthesis of a photoaffinity labeling analogue of the inactivating peptide of the Shaker B potassium channel.

A photoactivatable derivative of the inactivating peptide of the Shaker B potassium channel (ShB peptide) has been synthesized from ShB peptide containing an added cysteine residue at the peptide carboxy-terminus and 1-(p-azidosalicylamido)-4-(iodoacetamido)butane. The peptide derivative restores rapid inactivation in the deletion mutant Shaker Bdelta6-46 potassium channel in a manner indisting...

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ژورنال

عنوان ژورنال: Biochemistry

سال: 2003

ISSN: 0006-2960,1520-4995

DOI: 10.1021/bi0343121