How well can molecular modelling predict the crystal structure: The case of the ligand-binding domain of glutamate receptors

Yoav Paas; Anne Devillers-Thiéry; Vivian I. Teichberg; Jean Pierre Changeux; Miriam Eisenstein

doi:10.1016/s0165-6147(99)01443-1

How well can molecular modelling predict the crystal structure: The case of the ligand-binding domain of glutamate receptors

Yoav Paas, Anne Devillers-Thiéry, Vivian I. Teichberg, Jean Pierre Changeux, Miriam Eisenstein

The Mina and Everard Goodman Faculty of Life Sciences

Research output: Contribution to journal › Review article › peer-review

30 Scopus citations

Abstract

The concept that the ligand-binding domain of vertebrate glutamate receptor channels and bacterial periplasmic substrate-binding proteins (PBPs) share similar three-dimensional (3D) structures has gained increasing support in recent years. On the basis of a dual approach that included computer-assisted molecular modelling and functional studies of site-specific mutants, theoretical 3D models of this domain have been proposed. This article reviews to what extent these models could predict the crystal structure of the ligand-binding domain of an ionotropic glutamate receptor subunit recently determined at high resolution by X-ray diffraction studies. Copyright (C) 2000 Elsevier Science Ltd.

Original language	English
Pages (from-to)	87-92
Number of pages	6
Journal	Trends in Pharmacological Sciences
Volume	21
Issue number	3
DOIs	https://doi.org/10.1016/s0165-6147(99)01443-1
State	Published - 1 Mar 2000

Bibliographical note

Funding Information:
Y.P. is supported by a postdoctoral fellowship of the Human Frontier Science Program Organisation. The work by V.I.T. is supported by research grants from the German-Israel Foundation and Minerva Foundation. J.P.C. and A.D.T. thank the Collège de France, the EEC Biotech and Biomed Programs and the Association Française contre les Myopathies for support.

Funding

Y.P. is supported by a postdoctoral fellowship of the Human Frontier Science Program Organisation. The work by V.I.T. is supported by research grants from the German-Israel Foundation and Minerva Foundation. J.P.C. and A.D.T. thank the Collège de France, the EEC Biotech and Biomed Programs and the Association Française contre les Myopathies for support.

Funders	Funder number
Human Frontier Science Program
Minerva Foundation

Access to Document

10.1016/s0165-6147(99)01443-1

Cite this

@article{944b13ed39db47a49bf0250fb51fef32,

title = "How well can molecular modelling predict the crystal structure: The case of the ligand-binding domain of glutamate receptors",

abstract = "The concept that the ligand-binding domain of vertebrate glutamate receptor channels and bacterial periplasmic substrate-binding proteins (PBPs) share similar three-dimensional (3D) structures has gained increasing support in recent years. On the basis of a dual approach that included computer-assisted molecular modelling and functional studies of site-specific mutants, theoretical 3D models of this domain have been proposed. This article reviews to what extent these models could predict the crystal structure of the ligand-binding domain of an ionotropic glutamate receptor subunit recently determined at high resolution by X-ray diffraction studies. Copyright (C) 2000 Elsevier Science Ltd.",

author = "Yoav Paas and Anne Devillers-Thi{\'e}ry and Teichberg, {Vivian I.} and Changeux, {Jean Pierre} and Miriam Eisenstein",

note = "Funding Information: Y.P. is supported by a postdoctoral fellowship of the Human Frontier Science Program Organisation. The work by V.I.T. is supported by research grants from the German-Israel Foundation and Minerva Foundation. J.P.C. and A.D.T. thank the Coll{\`e}ge de France, the EEC Biotech and Biomed Programs and the Association Fran{\c c}aise contre les Myopathies for support. ",

year = "2000",

month = mar,

day = "1",

doi = "10.1016/s0165-6147(99)01443-1",

language = "אנגלית",

volume = "21",

pages = "87--92",

journal = "Trends in Pharmacological Sciences",

issn = "0165-6147",

publisher = "Elsevier Ltd.",

number = "3",

}

TY - JOUR

T1 - How well can molecular modelling predict the crystal structure

T2 - The case of the ligand-binding domain of glutamate receptors

AU - Paas, Yoav

AU - Devillers-Thiéry, Anne

AU - Teichberg, Vivian I.

AU - Changeux, Jean Pierre

AU - Eisenstein, Miriam

N1 - Funding Information: Y.P. is supported by a postdoctoral fellowship of the Human Frontier Science Program Organisation. The work by V.I.T. is supported by research grants from the German-Israel Foundation and Minerva Foundation. J.P.C. and A.D.T. thank the Collège de France, the EEC Biotech and Biomed Programs and the Association Française contre les Myopathies for support.

PY - 2000/3/1

Y1 - 2000/3/1

N2 - The concept that the ligand-binding domain of vertebrate glutamate receptor channels and bacterial periplasmic substrate-binding proteins (PBPs) share similar three-dimensional (3D) structures has gained increasing support in recent years. On the basis of a dual approach that included computer-assisted molecular modelling and functional studies of site-specific mutants, theoretical 3D models of this domain have been proposed. This article reviews to what extent these models could predict the crystal structure of the ligand-binding domain of an ionotropic glutamate receptor subunit recently determined at high resolution by X-ray diffraction studies. Copyright (C) 2000 Elsevier Science Ltd.

AB - The concept that the ligand-binding domain of vertebrate glutamate receptor channels and bacterial periplasmic substrate-binding proteins (PBPs) share similar three-dimensional (3D) structures has gained increasing support in recent years. On the basis of a dual approach that included computer-assisted molecular modelling and functional studies of site-specific mutants, theoretical 3D models of this domain have been proposed. This article reviews to what extent these models could predict the crystal structure of the ligand-binding domain of an ionotropic glutamate receptor subunit recently determined at high resolution by X-ray diffraction studies. Copyright (C) 2000 Elsevier Science Ltd.

UR - http://www.scopus.com/inward/record.url?scp=0002449713&partnerID=8YFLogxK

U2 - 10.1016/s0165-6147(99)01443-1

DO - 10.1016/s0165-6147(99)01443-1

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.systematicreview???

C2 - 10689361

AN - SCOPUS:0002449713

SN - 0165-6147

VL - 21

SP - 87

EP - 92

JO - Trends in Pharmacological Sciences

JF - Trends in Pharmacological Sciences

IS - 3

ER -

How well can molecular modelling predict the crystal structure: The case of the ligand-binding domain of glutamate receptors

Abstract

Bibliographical note

Funding

Access to Document

Other files and links

Fingerprint

Cite this