作者: J. P. Clancy , Zs. Bebök , E. J. Sorscher
关键词: Binding site 、 Nucleotide 、 Biochemistry 、 Cyclic nucleotide-binding domain 、 Chemistry 、 Binding domain 、 Cytoplasm 、 Biophysics 、 Molecular mass 、 Beta sheet 、 Ion transporter
摘要: The nucleotide binding domains (NBDs) within CFTR were initially predicted to lie in the cell cytoplasm, and gate anion permeability through a pore that was present membrane spanning α helices of overall polypeptide. Our studies designed characterize suggest several important features isolated domain. NBD-1 appears bind nucleotides with similar affinity full-length protein. In solution, domain contains high β sheet content self-associates into ordered polymers molecular mass greater than 300,000 Daltons. is very lipophilic, disrupts liposomes, readily enters planar lipid bilayer. Clinically mutations may disrupt capabilities protein, either direct effect on site, or effects influence folding vitro. Finally, after expression human epithelial cells (including from CF patient), first targets plasma even absence other constituents mediates these cells.