ATP binding site of P2X channel proteins:: structural similarities with class II aminoacyl-tRNA synthetases

被引：38

作者：

Freist, W ^{[1
]}

Verhey, JF ^{[1
]}

Stühmer, W ^{[1
]}

Gauss, DH ^{[1
]}

机构：

[1] Max Planck Inst Expt Med, D-37075 Gottingen, Germany

来源：

FEBS LETTERS | 1998年 / 434卷 / 1-2期

关键词：

ligand-gated channel; ATP receptor; purinoceptor; P2X; aminoacyl-tRNA synthetase;

D O I：

10.1016/S0014-5793(98)00958-2

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 extracellular loop of P2X channel proteins contains a sequence stretch (positions 170-330) that exhibits similarities with the catalytic domains of class II aminoacyl-tRNA synthetases as shown by secondary structure predictions and sequence alignments, The arrangement of several conserved cysteines (positions 110-170) shows similarities with metal binding regions of metallothioneins and zinc finger motifs. Thus, for the extracellular part of P2X channel proteins a metal binding domain and an antiparallel six-stranded beta-pleated sheet containing the ATP binding site are very probable. The putative channel forming H5 part (positions 320-340) shows similarities with the enzyme motif 1 responsible for aggregation of subunits to the holoenzyme, (C) 1998 Federation of European Biochemical Societies.

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页码：61 / 65

页数：5

相关论文

共 39 条

[1] Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase [J].

Aberg, A ;

Yaremchuk, A ;

Tukalo, M ;

Rasmussen, B ;

Cusack, S .

BIOCHEMISTRY, 1997, 36 (11) :3084-3094

[2] CRYSTAL-STRUCTURE OF HISTIDYL-TRANSFER-RNA SYNTHETASE FROM ESCHERICHIA-COLI COMPLEXED WITH HISTIDYL-ADENYLATE [J].

ARNEZ, JG ;

HARRIS, DC ;

MITSCHLER, A ;

REES, B ;

FRANCKLYN, CS ;

MORAS, D .

EMBO JOURNAL, 1995, 14 (17) :4143-4155

[3] THE STRUCTURAL BASIS FOR SERYL-ADENYLATE AND AP(4)A SYNTHESIS BY SERYL-TRANSFER-RNA SYNTHETASE [J].

BELRHALI, H ;

YAREMCHUK, A ;

TUKALO, M ;

BERTHETCOLOMINAS, C ;

RASMUSSEN, B ;

BOSECKE, P ;

DIAT, O ;

CUSACK, S .

STRUCTURE, 1995, 3 (04) :341-352

[4] CRYSTAL-STRUCTURES AT 2.5 ANGSTROM RESOLUTION OF SERYL-TRANSFER-RNA SYNTHETASE COMPLEXED 2 ANALOGS OF SERYL ADENYLATE [J].

BELRHALI, H ;

YAREMCHUK, A ;

TUKALO, M ;

LARSEN, K ;

BERTHETCOLOMINAS, C ;

LEBERMAN, R ;

BEIJER, B ;

SPROAT, B ;

ALSNIELSEN, J ;

GRUBEL, G ;

LEGRAND, JF ;

LEHMANN, M ;

CUSACK, S .

SCIENCE, 1994, 263 (5152) :1432-1436

[5] Signaling by extracellular nucleotides [J].

Brake, AJ ;

Julius, D .

ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1996, 12 :519-541

[6] NEW STRUCTURAL MOTIF FOR LIGAND-GATED ION CHANNELS DEFINED BY AN IONOTROPIC ATP RECEPTOR [J].

BRAKE, AJ ;

WAGENBACH, MJ ;

JULIUS, D .

NATURE, 1994, 371 (6497) :519-523

[7] P2X receptors: An emerging channel family [J].

Buell, G ;

Collo, G ;

Rassendren, F .

EUROPEAN JOURNAL OF NEUROSCIENCE, 1996, 8 (10) :2221-2228

[8]

BURBAUM JJ, 1991, J BIOL CHEM, V266, P16965

[9] THE ACTIVE-SITE OF YEAST ASPARTYL-TRANSFER-RNA SYNTHETASE - STRUCTURAL AND FUNCTIONAL-ASPECTS OF THE AMINOACYLATION REACTION [J].

CAVARELLI, J ;

ERIANI, G ;

REES, B ;

RUFF, M ;

BOEGLIN, M ;

MITSCHLER, A ;

MARTIN, F ;

GANGLOFF, J ;

THIERRY, JC ;

MORAS, D .

EMBO JOURNAL, 1994, 13 (02) :327-337

[10] YEAST TRANSFER RNA(ASP) RECOGNITION BY ITS COGNATE CLASS-II AMINOACYL-TRANSFER RNA-SYNTHETASE [J].

CAVARELLI, J ;

REES, B ;

RUFF, M ;

THIERRY, JC ;

MORAS, D .

NATURE, 1993, 362 (6416) :181-184

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