Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints

Karen L. Martinez; Yann Gohon; Pierre Jean Corringer; Christophe Tribet; Fabienne Mérola; Jean Pierre Changeux; Jean Luc Popot

doi:10.1016/S0014-5793(02)03306-9

Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints

Karen L. Martinez, Yann Gohon, Pierre Jean Corringer, Christophe Tribet, Fabienne Mérola, Jean Pierre Changeux, Jean Luc Popot^*

^*Corresponding author af dette arbejde

Kemisk Institut

53 Citationer (Scopus)

Abstract

The binding of a fluorescent agonist to the acetycholine receptor from Torpedo electric organ has been studied by time-resolved spectroscopy in three different environments: in native membrane fragments, in the detergent CHAPS, and after complexation by amphipathic polymers ('amphipols'). Binding kinetics was similar in the membrane and in amphipols, demonstrating that the receptor can display unaltered allosteric transitions outside its natural lipid environment. In contrast, allosteric equilibria were strongly shifted towards the desensitized state in CHAPS. Therefore, the effect of CHAPS likely results from molecular interactions rather than from the loss of bulk physical properties of the membrane environment.

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	528
Udgave nummer	1-3
Sider (fra-til)	251-256
Antal sider	6
ISSN	0014-5793
DOI	https://doi.org/10.1016/S0014-5793(02)03306-9
Status	Udgivet - 25 sep. 2002

Adgang til dokumentet

10.1016/S0014-5793(02)03306-9

http://www.scopus.com/inward/record.url?scp=0037174145&partnerID=8YFLogxK

Citationsformater

@article{982a523f2fbe4b59a9111be7f516008f,

title = "Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints",

abstract = "The binding of a fluorescent agonist to the acetycholine receptor from Torpedo electric organ has been studied by time-resolved spectroscopy in three different environments: in native membrane fragments, in the detergent CHAPS, and after complexation by amphipathic polymers ('amphipols'). Binding kinetics was similar in the membrane and in amphipols, demonstrating that the receptor can display unaltered allosteric transitions outside its natural lipid environment. In contrast, allosteric equilibria were strongly shifted towards the desensitized state in CHAPS. Therefore, the effect of CHAPS likely results from molecular interactions rather than from the loss of bulk physical properties of the membrane environment.",

keywords = "Amphipol, Conformational transition, Detergent, Membrane protein, Nicotinic acetylcholine receptor",

author = "Martinez, {Karen L.} and Yann Gohon and Corringer, {Pierre Jean} and Christophe Tribet and Fabienne M{\'e}rola and Changeux, {Jean Pierre} and Popot, {Jean Luc}",

year = "2002",

month = sep,

day = "25",

doi = "10.1016/S0014-5793(02)03306-9",

language = "English",

volume = "528",

pages = "251--256",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "1-3",

}

TY - JOUR

T1 - Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols

T2 - Molecular interactions vs. physical constraints

AU - Martinez, Karen L.

AU - Gohon, Yann

AU - Corringer, Pierre Jean

AU - Tribet, Christophe

AU - Mérola, Fabienne

AU - Changeux, Jean Pierre

AU - Popot, Jean Luc

PY - 2002/9/25

Y1 - 2002/9/25

N2 - The binding of a fluorescent agonist to the acetycholine receptor from Torpedo electric organ has been studied by time-resolved spectroscopy in three different environments: in native membrane fragments, in the detergent CHAPS, and after complexation by amphipathic polymers ('amphipols'). Binding kinetics was similar in the membrane and in amphipols, demonstrating that the receptor can display unaltered allosteric transitions outside its natural lipid environment. In contrast, allosteric equilibria were strongly shifted towards the desensitized state in CHAPS. Therefore, the effect of CHAPS likely results from molecular interactions rather than from the loss of bulk physical properties of the membrane environment.

AB - The binding of a fluorescent agonist to the acetycholine receptor from Torpedo electric organ has been studied by time-resolved spectroscopy in three different environments: in native membrane fragments, in the detergent CHAPS, and after complexation by amphipathic polymers ('amphipols'). Binding kinetics was similar in the membrane and in amphipols, demonstrating that the receptor can display unaltered allosteric transitions outside its natural lipid environment. In contrast, allosteric equilibria were strongly shifted towards the desensitized state in CHAPS. Therefore, the effect of CHAPS likely results from molecular interactions rather than from the loss of bulk physical properties of the membrane environment.

KW - Amphipol

KW - Conformational transition

KW - Detergent

KW - Membrane protein

KW - Nicotinic acetylcholine receptor

U2 - 10.1016/S0014-5793(02)03306-9

DO - 10.1016/S0014-5793(02)03306-9

M3 - Journal article

C2 - 12297315

AN - SCOPUS:0037174145

SN - 0014-5793

VL - 528

SP - 251

EP - 256

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints

Abstract

Adgang til dokumentet

Fingeraftryk

Citationsformater