FEBS Letters | |
A two‐domain model for the R domain of the cystic fibrosis transmembrane conductance regulator based on sequence similarities | |
Riordan, John R.1  Dulhanty, Ann M.1  | |
[1] Cystic Fibrosis Research Development Program and Biochemistry Department, Hospital for Sick Children, 555 University Ave., Toronto, Ont., M5G 1X8, Canada | |
关键词: Alignment; CFTR; Retrovirus; Homology; Pol protein; CFTR; cystic fibrosis transmembrane conductance regulator protein; PKA; cAMP dependent protein kinase; PKC; protein kinase C; NBF; nucleotide binding fold; PIR; Protein Resource Information; MMLV; Moloney murine leukemia virus; | |
DOI : 10.1016/0014-5793(94)80300-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 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.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020299441ZK.pdf | 961KB | download |