(Q28212998)

English

Modeling the structure of agitoxin in complex with the Shaker K+ channel: a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles

scientific article (publication date: November 2002)

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scholarly article

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Modeling the structure of agitoxin in complex with the Shaker K+ channel: a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles (English)

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author name string

Mats A L Eriksson

1

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Benoît Roux

2

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language of work or name

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publication date

November 2002

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Biophysical Journal

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83

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2595-609

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5

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Crystal structure and mechanism of a calcium-gated potassium channel

1 reference

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Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution

1 reference

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Protein docking along smooth association pathways

1 reference

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Brownian dynamics simulations of interaction between scorpion toxin Lq2 and potassium ion channel.

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The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

1 reference

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On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures

1 reference

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Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone

1 reference

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Principles of protein-protein interactions

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Structure-guided transformation of charybdotoxin yields an analog that selectively targets Ca(2+)-activated over voltage-gated K(+) channels.

1 reference

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1 reference

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1 reference

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Helical structure and packing orientation of the S2 segment in the Shaker K+ channel

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The activation gate of a voltage-gated K+ channel can be trapped in the open state by an intersubunit metal bridge

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Structural implications of fluorescence quenching in the Shaker K+ channel

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Structural conservation in prokaryotic and eukaryotic potassium channels

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Recent studies on dendrotoxins and potassium ion channels

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Molecular properties of voltage-gated K+ channels

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A symmetry-driven search for electrostatic interaction partners in charybdotoxin and a voltage-gated K+ channel

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Side-chain conformational entropy in protein folding

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A strongly interacting pair of residues on the contact surface of charybdotoxin and a Shaker K+ channel.

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Mutations in the K+ channel signature sequence

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Electrostatic distance geometry in a K+ channel vestibule

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Identifiers

10.1016/S0006-3495(02)75270-3

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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