Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis. (Q52546897)

3 May 2018

title

Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis. (English)

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3 May 2018

author name string

Ranganathan R

series ordinal

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3 May 2018

Lewis JH

series ordinal

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3 May 2018

MacKinnon R

series ordinal

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3 May 2018

language of work or name

English

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publication date

1 January 1996

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3 May 2018

published in

Neuron

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3 May 2018

volume

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3 May 2018

issue

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3 May 2018

page(s)

131-139

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3 May 2018

Topology of the pore-region of a K+ channel revealed by the NMR-derived structures of scorpion toxins

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Charybdotoxin block of single Ca2+-activated K+ channels. Effects of channel gating, voltage, and ionic strength

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Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect Defensins

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Influence of protein surface charge on the bimolecular kinetics of a potassium channel peptide inhibitor

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Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom

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The charybdotoxin receptor of a Shaker K+ channel: peptide and channel residues mediating molecular recognition

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Agitoxin footprinting the shaker potassium channel pore

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The aromatic binding site for tetraethylammonium ion on potassium channels

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Mutations in the K+ channel signature sequence

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Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor.

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Biophysical and molecular mechanisms of Shaker potassium channel inactivation

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Determination of the three-dimensional structure of iberiotoxin in solution by 1H nuclear magnetic resonance spectroscopy

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Molecular characterization of Shaker, a Drosophila gene that encodes a potassium channel

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Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry

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A conductance maximum observed in an inward-rectifier potassium channel

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Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel

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The charybdotoxin family of K+ channel-blocking peptides

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Interaction of charybdotoxin with permeant ions inside the pore of a K+ channel.

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Design, synthesis, and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels

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Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles

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Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin

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Electrostatic distance geometry in a K+ channel vestibule

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Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel.

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Identifiers

DOI

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3 May 2018

1 reference

3 May 2018