DESIGN OF MOLECULAR FUNCTION - CHANNELS OF COMMUNICATION

被引:71
作者
MONTAL, M
机构
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1995年 / 24卷
关键词
DE NOVO PROTEIN DESIGN; PROTEIN FOLDING; MEMBRANE-PROTEIN STRUCTURE; IONIC CHANNELS; NEUROTRANSMITTER RECEPTORS; LIPID BILAYERS;
D O I
10.1146/annurev.biophys.24.1.31
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ultimate goal in protein design is to elucidate the fundamental principles that determine structure. With increased understanding of the molecular basis underlying the sequence-structure relationship may come the ability to control it and, thereby, to generate proteins with desired specifications. Channel proteins, which mediate cell signaling, are ideally suitable for protein design. Plausible molecular blueprints for the pore-forming structure are bundles of amphipathic alpha-helices or beta-barrels that cluster together to generate a hydrophilic channel. This review focuses on the progress achieved to produce such designs and on the approximation of the synthetic channels to the targeted biological function.
引用
收藏
页码:31 / 57
页数:27
相关论文
共 122 条
[1]   ACETYLCHOLINE-RECEPTOR CHANNEL STRUCTURE PROBED IN CYSTEINE-SUBSTITUTION MUTANTS [J].
AKABAS, MH ;
STAUFFER, DA ;
XU, M ;
KARLIN, A .
SCIENCE, 1992, 258 (5080) :307-310
[2]   SYNTHETIC PEPTIDES AS MODELS FOR ION CHANNEL PROTEINS [J].
AKERFELDT, KS ;
LEAR, JD ;
WASSERMAN, ZR ;
CHUNG, LA ;
DEGRADO, WF .
ACCOUNTS OF CHEMICAL RESEARCH, 1993, 26 (04) :191-197
[3]  
ATTALI B, 1993, J BIOL CHEM, V268, P24283
[4]   ASSEMBLY OF MAMMALIAN VOLTAGE-GATED POTASSIUM CHANNELS - EVIDENCE FOR AN IMPORTANT ROLE OF THE FIRST TRANSMEMBRANE SEGMENT [J].
BABILA, T ;
MOSCUCCI, A ;
WANG, HY ;
WEAVER, FE ;
KOREN, G .
NEURON, 1994, 12 (03) :615-626
[5]  
BECHINGER B, 1991, Journal of Biomolecular NMR, V1, P167, DOI 10.1007/BF01877228
[6]   STRUCTURE-FUNCTION ANALYSIS OF THE ION-CHANNEL SELECTIVITY FILTER IN HUMAN ANNEXIN-V [J].
BERENDES, R ;
VOGES, D ;
DEMANGE, P ;
HUBER, R ;
BURGER, A .
SCIENCE, 1993, 262 (5132) :427-430
[7]   MUTATIONS AT 2 DISTINCT SITES WITHIN THE CHANNEL DOMAIN M2 ALTER CALCIUM PERMEABILITY OF NEURONAL ALPHA-7 NICOTINIC RECEPTOR [J].
BERTRAND, D ;
GALZI, JL ;
DEVILLERSTHIERY, A ;
BERTRAND, S ;
CHANGEUX, JP .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (15) :6971-6975
[8]   STRUCTURE AND FUNCTION OF INHIBITORY GLYCINE RECEPTORS [J].
BETZ, H .
QUARTERLY REVIEWS OF BIOPHYSICS, 1992, 25 (04) :381-394
[9]   VOLTAGE-DEPENDENT GATING OF IONIC CHANNELS [J].
BEZANILLA, F ;
STEFANI, E .
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1994, 23 :819-846
[10]   RESIDUES WITHIN TRANSMEMBRANE SEGMENT M2 DETERMINE CHLORIDE CONDUCTANCE OF GLYCINE RECEPTOR HOMO-OLIGOMERS AND HETEROOLIGOMERS [J].
BORMANN, J ;
RUNDSTROM, N ;
BETZ, H ;
LANGOSCH, D .
EMBO JOURNAL, 1993, 12 (10) :3729-3737