Glutamate receptors: variation in structure-function coupling

Anders Skov Kristensen; Matthew Geballe; James P Snyder; Stephen F Traynelis

Glutamate receptors: variation in structure-function coupling

Anders Skov Kristensen, Matthew Geballe, James P Snyder, Stephen F Traynelis

5 Citations (Scopus)

Abstract

Fast excitatory synaptic transmission in the CNS relies almost entirely on the neurotransmitter glutamate and its family of ion channel receptors. An appreciation of the coupling between agonist binding and channel opening has advanced rapidly during the past five years, largely as a result of new structural information about the agonist-binding site. Recent studies suggest that despite many structural similarities different family members use different mechanisms to translate agonist binding into channel opening.

Original language	English
Journal	Trends in Pharmacological Sciences
Volume	27
Issue number	2
Pages (from-to)	65-69
Number of pages	5
ISSN	0165-6147
Publication status	Published - Feb 2006

Cite this

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title = "Glutamate receptors: variation in structure-function coupling",

abstract = "Fast excitatory synaptic transmission in the CNS relies almost entirely on the neurotransmitter glutamate and its family of ion channel receptors. An appreciation of the coupling between agonist binding and channel opening has advanced rapidly during the past five years, largely as a result of new structural information about the agonist-binding site. Recent studies suggest that despite many structural similarities different family members use different mechanisms to translate agonist binding into channel opening.",

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AU - Geballe, Matthew

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AU - Traynelis, Stephen F

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AB - Fast excitatory synaptic transmission in the CNS relies almost entirely on the neurotransmitter glutamate and its family of ion channel receptors. An appreciation of the coupling between agonist binding and channel opening has advanced rapidly during the past five years, largely as a result of new structural information about the agonist-binding site. Recent studies suggest that despite many structural similarities different family members use different mechanisms to translate agonist binding into channel opening.

M3 - Journal article

SN - 0165-6147

VL - 27

SP - 65

EP - 69

JO - Trends in Pharmacological Sciences

JF - Trends in Pharmacological Sciences

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ER -