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ATP binding site of P2X channel proteins: structural similarities with class II aminoacyl‐tRNA synthetases
Author(s) -
Freist Wolfgang,
Verhey Janko F,
Stühmer Walter,
Gauss Dieter H
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00958-2
Subject(s) - antiparallel (mathematics) , aminoacyl trna synthetase , zinc finger , structural motif , binding site , biochemistry , sequence motif , transfer rna , sequence alignment , protein structure , sequence (biology) , biology , chemistry , peptide sequence , biophysics , dna , rna , transcription factor , physics , quantum mechanics , magnetic field , gene
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 β‐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.