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Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor

Article Abstract:

Chemical modification, electrophysiology, and crystallography experiments were applied to study the conformational rearrangements of the extracellular glutamate-binding core subunits that accompany receptor desensitization. The study results demonstrate that desensitization involves the rupture of an extensive interface between domain 1 of 2-fold related glutamate-binding core subunits, compensating for the ca. 21 degree of domain closure induced by glutamate binding.

Author: Gouaux, Eric, Jasti, Jaysankar, Armstrong, Neali, Beich-Frandsen, Mads
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
Glutamate, Desensitization (Psychotherapy)

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Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K(super +) channel

Article Abstract:

The membrane depth of residues throughout the KvAP channel, a voltage-dependent K(super +) channel, is measured using avidin accessibility to different-length tethered biotin reagents. From these measurements the lengths are calibrated and the thickness of the membrane that forms a barrier to avidin penetration is derived to determine the magnitude of displacement of the arginine residues in the voltage-sensor paddles during channel gating.

Author: Ruta, Vanessa, Jiyayun Chen, Mackinnon, Roderick
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2005
Arginine, Biotin

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Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain

Article Abstract:

The crystal structure of the HERG K+ channel N-terminal domain was characterized and its function as a modifier of gating was investigated utilizing electrophysiological procedures. The domain resembles in structure a bacterial light sensor photoactive yellow protein and offers the first three-dimensional model of a eukaryotic PAS domain. The presence of the domain linked to the channel slows the rate of deactivation.

Author: Li, Min, Chait, Brian T., Lee, Alice, Mackinnon, Roderick, Cohen, Steven L., Cabral, Joao H. Morais
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Genetic aspects, Eukaryotic cells, Cells (Biology), Eukaryotes, Potassium channels

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Subjects list: Research
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