CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices

@article{Baker2007CFTRRR,
  title={CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices},
  author={Jennifer M R Baker and Rhea P. Hudson and Voula Kanelis and Wing-Yiu Choy and Patrick H Thibodeau and Philip J. Thomas and Julie Deborah Forman-Kay},
  journal={Nature Structural &Molecular Biology},
  year={2007},
  volume={14},
  pages={738-745}
}
The regulatory (R) region of the cystic fibrosis transmembrane conductance regulator (CFTR) is intrinsically disordered and must be phosphorylated at multiple sites for full CFTR channel activity, with no one specific phosphorylation site required. In addition, nucleotide binding and hydrolysis at the nucleotide-binding domains (NBDs) of CFTR are required for channel gating. We report NMR studies in the absence and presence of NBD1 that provide structural details for the isolated R region and… CONTINUE READING
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