Agitoxin footprinting the Shaker potassium channel pore

156Citations
Citations of this article
57Readers
Mendeley users who have this article in their library.

Abstract

In voltage-dependent K+ channels, each of the four identical subunits contributes one pore loop to the central ion selectivity unit at the interface between the subunits. The pore loop is also the target for scorpion venom peptide inhibitors. These inhibitors bind at the pore entryway between the four subunits and can assume any one of four orientations. The orientations become distinguishable only if the binding site symmetry is disrupted. We have used mutagenesis and site-directed chemical modification to alter pore loop amino acids in either one or four subunits. The effects of these alterations on inhibitor affinity define the eccentricity of amino acids in the pore entryway and imply a different secondary structure for the amino and carboxyl ends of the pore loop.

Cite

CITATION STYLE

APA

Gross, A., & MacKinnon, R. (1996). Agitoxin footprinting the Shaker potassium channel pore. Neuron, 16(2), 399–406. https://doi.org/10.1016/S0896-6273(00)80057-4

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free