[HTML][HTML] The molecular chaperone Hsc70 assists the in VitroFolding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance …
E Strickland, BH Qu, L Millen, PJ Thomas - Journal of Biological Chemistry, 1997 - ASBMB
The most common disease-causing mutation in the cystic fibrosis transmembrane
conductance regulator is a single amino acid deletion (ΔF508) in the N-terminal cytosolic
nucleotide-binding domain (NBD1). This mutation has previously been shown to be a
temperature-sensitive folding mutation that alters the folding pathway but not the native state
stability of the isolated domain (Qu, B.-H., and Thomas, PJ (1996) J. Biol. Chem. 271, 7261–
7264). Here we provide evidence that the molecular chaperone Hsc70 productively interacts …
conductance regulator is a single amino acid deletion (ΔF508) in the N-terminal cytosolic
nucleotide-binding domain (NBD1). This mutation has previously been shown to be a
temperature-sensitive folding mutation that alters the folding pathway but not the native state
stability of the isolated domain (Qu, B.-H., and Thomas, PJ (1996) J. Biol. Chem. 271, 7261–
7264). Here we provide evidence that the molecular chaperone Hsc70 productively interacts …
