IMPORTANCE OF THE MEMBRANE IN LIGAND RECEPTOR INTERACTIONS

被引：10

作者：

BEHLING, RW ^{[1
]}

JELINSKI, LW ^{[1
]}

机构：

[1] AT&T BELL LABS,MURRAY HILL,NJ 07974

来源：

BIOCHEMICAL PHARMACOLOGY | 1990年 / 40卷 / 01期

关键词：

D O I：

10.1016/0006-2952(90)90177-M

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

NMR data that underscore the importance of the membrane in ligand-receptor interactions were obtained and analyzed. The following hypothesis for acetylcholine (ACh) binding to the acetyicholine receptor (AChR) is proposed: ACh first binds to the membrane, where it adopts its bioactive conformation, and it then rapidly diffuses along the membrane to bind to the AChR in its already-correct conformation. Data used to support this hypothesis include (a) the NMR-determined binding constant of KM = (2.8 ± 0.6) × 103 M-1 for the binding of ACh to the asolectin membrane, (b) the lipid dependence of AChR activity, (c) the location of the ACh binding site close to the membrane surface, and (d) the conformation of ACh in its membrane-bound state. Additional experiments to test this hypothesis are proposed. © 1990.

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页码：49 / 54

页数：6

相关论文

共 35 条

[1] MAPPING THE MAIN IMMUNOGENIC REGION AND TOXIN-BINDING SITE OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR [J].

BARKAS, T ;

MAURON, A ;

ROTH, B ;

ALLIOD, C ;

TZARTOS, SJ ;

BALLIVET, M .

SCIENCE, 1987, 235 (4784) :77-80

[2] MEASURING RELATIVE ACETYLCHOLINE-RECEPTOR AGONIST BINDING BY SELECTIVE PROTON NUCLEAR MAGNETIC-RESONANCE RELAXATION EXPERIMENTS [J].

BEHLING, RW ;

YAMANE, T ;

NAVON, G ;

SAMMON, MJ ;

JELINSKI, LW .

BIOPHYSICAL JOURNAL, 1988, 53 (06) :947-954

[3] CONFORMATION OF ACETYLCHOLINE BOUND TO THE NICOTINIC ACETYLCHOLINE-RECEPTOR [J].

BEHLING, RW ;

YAMANE, T ;

NAVON, G ;

JELINSKI, LW .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (18) :6721-6725

[4]

BEVERIDGE DL, 1973, 1972 P INT S HELD JE, P481

[5] KINETICS OF BINDING OF [ACETYLCHOLINE-H-3 TO TORPEDO POSTSYNAPTIC MEMBRANES - ASSOCIATION AND DISSOCIATION RATE CONSTANTS BY RAPID MIXING AND ULTRAFILTRATION [J].

BOYD, ND ;

COHEN, JB .

BIOCHEMISTRY, 1980, 19 (23) :5353-5358

[6] PREDICTION OF THE FOLDING OF SHORT POLYPEPTIDE SEGMENTS BY UNIFORM CONFORMATIONAL SAMPLING [J].

BRUCCOLERI, RE ;

KARPLUS, M .

BIOPOLYMERS, 1987, 26 (01) :137-168

[7] DIFFUSION OF DIHYDROPYRIDINE CALCIUM-CHANNEL ANTAGONISTS IN CARDIAC SARCOLEMMAL LIPID MULTIBILAYERS [J].

CHESTER, DW ;

HERBETTE, LG ;

MASON, RP ;

JOSLYN, AF ;

TRIGGLE, DJ ;

KOPPEL, DE .

BIOPHYSICAL JOURNAL, 1987, 52 (06) :1021-1030

[8] HYDROPHOBIC BONDING AND ACCESSIBLE SURFACE-AREA IN PROTEINS [J].

CHOTHIA, C .

NATURE, 1974, 248 (5446) :338-339

[9] EVIDENCE THAT THE ACETYLCHOLINE BINDING-SITE IS NOT FORMED BY THE SEQUENCE ALPHA-127-143 OF THE ACETYLCHOLINE-RECEPTOR [J].

CRIADO, M ;

SARIN, V ;

FOX, JL ;

LINDSTROM, J .

BIOCHEMISTRY, 1986, 25 (10) :2839-2846

[10] A PHOTOAFFINITY LIGAND OF THE ACETYLCHOLINE-BINDING SITE PREDOMINANTLY LABELS THE REGION 179-207 OF THE ALPHA-SUBUNIT ON NATIVE ACETYLCHOLINE-RECEPTOR FROM TORPEDO-MARMORATA [J].

DENNIS, M ;

GIRAUDAT, J ;

KOTZYBAHIBERT, F ;

GOELDNER, M ;

HIRTH, C ;

CHANG, JY ;

CHANGEUX, JP .

FEBS LETTERS, 1986, 207 (02) :243-249

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