A 2-DOMAIN MODEL FOR THE R-DOMAIN OF THE CYSTIC-FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR BASED ON SEQUENCE SIMILARITIES

被引：28

作者：

DULHANTY, AM ^{[1
]}

RIORDAN, JR ^{[1
]}

机构：

[1] HOSP SICK CHILDREN,DEPT BIOCHEM,TORONTO M5G 1X8,ON,CANADA

来源：

FEBS LETTERS | 1994年 / 343卷 / 02期

关键词：

ALIGNMENT; CFTR; RETROVIRUS; HOMOLOGY; POL PROTEIN;

D O I：

10.1016/0014-5793(94)80300-5

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：

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.

引用

页码：109 / 114

页数：6

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