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Nucleotide-binding domain 1 (NBD1), one of two ABC domains in CFTR, also contains sites for the predominant CF-causing mutation and, potentially, for regulatory phosphorylation.
Cystic fibrosis is an inherited disease caused by mutations in a gene called the cystic fibrosis transmembrane conductance regulator (CFTR). The CFTR gene provides instructions for the CFTR protein . People who inherit two copies of a mutated CFTR gene (one copy from each biological parent) will have cystic fibrosis.
CFTR consists of two transmembrane domains, two nucleotide-binding domains (NBD1 and NBD2), and a regulatory domain. Previous biochemical reports suggest NBD1 is a site of stable nucleotide interaction with low ATPase activity, whereas NBD2 is the site of active ATP hydrolysis.
The cystic fibrosis transmembrane conductance regulator (CFTR) protein helps to maintain the balance of salt and water on many surfaces in the body, such as the surface of the lung. When the protein is not working correctly, chloride a component of salt becomes trapped in cells.
The most common CF mutation, F508del, is primarily considered to be a processing mutation. The F508del mutation removes a single amino acid from the CFTR protein. Without this building block, the CFTR protein cannot stay in the correct 3-D shape.
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Recombinant peptide is a manipulated form of peptide encoded by recombinant DNA, which has been cloned in a foreign expression system to supports the expression of the exogenous gene. This recombinant DNA construct can be used to manufacture large quantities of useful protein products.
A recombinant peptide therapy is produced through recombinant DNA technology. This involves inserting the DNA encoding the peptide into bacterial or mammalian cells, expressing the peptide in these cells and then purifying it from them.

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