Article
The cystic fibrosis transmembrane conductance regulator. Overexpression, purification, and characterization of wild type and delta F508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein.
The Journal of biological chemistry - 15 Nov 1993
Ko Y H, Thomas P J, Delannoy M R, Pedersen P L
Abstract excerpt
The first nucleotide binding fold (NBF1) of the cystic fibrosis transmembrane conductance regulator (CFTR) and its disease-causing mutant form (delta F508,NBF1) were overexpressed in high yield in Escherichia coli in fusion with the maltose-binding protein (MBP). The rationale for producing the chimerae was to aid in domain purification, solubilization, and crystallization and to examine the effect of...
Topics
- ATP-Binding Cassette Transporters
- Adenosine Triphosphate
- Base Sequence
- Binding Sites
- Carrier Proteins
- Chromatography, Gel
- Cloning, Molecular
- Crystallization
- Cystic Fibrosis
- Cystic Fibrosis Transmembrane Conductance Regulator