The macro- and microarchitectures of the ligand-binding domain of glutamate receptors

Yoav Paas

doi:10.1016/s0166-2236(97)01184-3

The macro- and microarchitectures of the ligand-binding domain of glutamate receptors

Yoav Paas

CNRS

Research output: Contribution to journal › Article › peer-review

89 Scopus citations

Abstract

Over the last decade, a large body of information regarding the amino acid sequences and tertiary structures of many proteins has accumulated. Subtle similarities in sequence patterns identified between glutamate receptors and bacterial periplasmic substrate-binding proteins have suggested that structural kinship exists between these protein families. Many of the bacterial periplasmic binding proteins but none of the glutamate receptors have been crystallized so far. The following article reviews how the resemblance between these two protein families led to computer-assisted structural models of crucial elements involved in ligand binding by various glutamate receptors. A plausible dynamic model of the molecular mechanism of activation and desensitization of glutamate-receptor channels is also discussed.

Original language	English
Pages (from-to)	117-125
Number of pages	9
Journal	Trends in Neurosciences
Volume	21
Issue number	3
DOIs	https://doi.org/10.1016/s0166-2236(97)01184-3
State	Published - 1 Mar 1998
Externally published	Yes

Bibliographical note

Funding Information:
I wish to thank Jean-Pierre Changeux for critically reading the manuscript, stimulating discussion and his unfailing support; Lisa Marubio, Anne Devillers-Thiéry and Stuart J. Edelstein for critical reading of the manuscript and Pierre-Jean Corringer, Clément Léna and Vivian I. Teichberg for their judicious advice. This work was supported by long-term fellowships from the Federation of European Biochemical Societies and the Human Frontier Science Program Organization.

Funding

I wish to thank Jean-Pierre Changeux for critically reading the manuscript, stimulating discussion and his unfailing support; Lisa Marubio, Anne Devillers-Thiéry and Stuart J. Edelstein for critical reading of the manuscript and Pierre-Jean Corringer, Clément Léna and Vivian I. Teichberg for their judicious advice. This work was supported by long-term fellowships from the Federation of European Biochemical Societies and the Human Frontier Science Program Organization.

Funders	Funder number
Human Frontier Science Program Organization
Federation of European Biochemical Societies

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10.1016/s0166-2236(97)01184-3

Cite this

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title = "The macro- and microarchitectures of the ligand-binding domain of glutamate receptors",

abstract = "Over the last decade, a large body of information regarding the amino acid sequences and tertiary structures of many proteins has accumulated. Subtle similarities in sequence patterns identified between glutamate receptors and bacterial periplasmic substrate-binding proteins have suggested that structural kinship exists between these protein families. Many of the bacterial periplasmic binding proteins but none of the glutamate receptors have been crystallized so far. The following article reviews how the resemblance between these two protein families led to computer-assisted structural models of crucial elements involved in ligand binding by various glutamate receptors. A plausible dynamic model of the molecular mechanism of activation and desensitization of glutamate-receptor channels is also discussed.",

author = "Yoav Paas",

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The macro- and microarchitectures of the ligand-binding domain of glutamate receptors

Abstract

Bibliographical note

Funding

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