A two‐domain model for the R domain of the cystic fibrosis transmembrane conductance regulator based on sequence similarities

FEBS Letters

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