EC Number   |
Subunits |
Reference |
|---|
   5.6.1.6 | ? |
x * 140000-150000, recombinant mutant DELTAPhe508, SDS-PAGE |
700296 |
| 5.6.1.6 | ? |
x * 150000, SDS-PAGE |
750504 |
| 5.6.1.6 | ? |
x * 150000-170000, fully glycosylated DELTAF508-CFTR, SDS-PAGE |
210426 |
| 5.6.1.6 | ? |
x * 160000, SDS-PAGE |
-, 734544 |
| 5.6.1.6 | ? |
x * 180000, untagged CFTR, SDS-PAGE, x * 210000, GFP-tagged CFTR, SDS-PAGE |
695466 |
| 5.6.1.6 | monomer |
1 * 170000, CFTR exitsts as monomers and multimers, the monomer is the minimum functional unit required for channel and ATPase activity, SDS-PAGE |
654579 |
| 5.6.1.6 | More |
CFTR is a polytopic membrane protein that functions as a Cl- channel and consists of two membrane spanning domains, two cytosolic nucleotide binding domains, and a cytosolic regulatory domain. The assembly of CFTR into an ion channel is complicated because it requires the coordinated folding and assembly of its membrane and cytoplasmic domains into a functional unit. Misfolding of CFTR and analysis by trypsin proteolysis patterns of misfolded CFTR, model of calnexin action in CFTR folding, overview |
700093 |
| 5.6.1.6 | More |
CFTR is composed of five domains: two membrane-spanning domains which form the channel pore, two nucleotide-binding domains and a regulatory R domain. Phosphorylation of the R domain determines channel activity, ATP hydrolysis by the nucleotide-binding domains controls gating |
210422 |
| 5.6.1.6 | More |
comparison of CFTR protein sequences to those of other ABC transporters, structure analysis, overview. A residue, identified as being involved in CFTR functional divergence, by virtue of being both CFTR-specific and conserved among all CFTR orthologs, is R352 in the sixth transmembrane helix, TM6. R352 interacts with absolutely conserved D993 in TM9 to stabilize the open-channel state |
700965 |
| 5.6.1.6 | More |
construction of a putative molecular three-dimensional model of the nucleotide-binding domain 1-nucleotide-binding domain 2 heterodimer |
734231 |
