Structural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteins.

@article{Carson1995StructuralAF,
  title={Structural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteins.},
  author={Mark Carson and Michael J. Welsh},
  journal={Biophysical journal},
  year={1995},
  volume={69 6},
  pages={2443-8}
}
The opening and closing of the CFTR Cl- channel are regulated by ATP hydrolysis at its two nucleotide binding domains (NBDs). However, the mechanism and functional significance of ATP hydrolysis are unknown. Sequence similarity between the NBDs of CFTR and GTP-binding proteins suggested the NBDs might have a structure and perhaps a function like that of GTP-binding proteins. Based on this similarity, we predicted that the terminal residue of the LSGGQ motif in the NBDs of CFTR corresponds to a… CONTINUE READING