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A two‐domain model for the R domain of the cystic fibrosis transmembrane conductance regulator based on sequence similarities
Author(s) -
Dulhanty Ann M.,
Riordan John R.
Publication year - 1994
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 - 10.1016/0014-5793(94)80300-5
Subject(s) - cystic fibrosis transmembrane conductance regulator , cyclic nucleotide binding domain , hamp domain , transmembrane domain , domain (mathematical analysis) , egf like domain , cytoplasm , transmembrane protein , peptide sequence , protein domain , sequence (biology) , biology , chemistry , biophysics , genetics , amino acid , cystic fibrosis , gene , mathematics , mathematical analysis , receptor
CFTR belongs to a group of proteins sharing the structural motif of six transmembrane helices and a nucleotide binding domain. Unique to CFTR is the R domain, a charged cytoplasmic domain. Comparison of R domain sequences from ten species revealed that the N‐terminal third is highly conserved, while the C‐terminal two‐thirds is poorly conserved. The R domain shows no strong sequence similarity to known proteins; however, 14 viral pol proteins show limited similarity to fragments of the R domain. Analysis revealed a relationship between the N‐ and C‐terminal fragments of the R domain and two discontinuous fragments of the pol protein. These observations support a two‐domain model for the R domain.