The stability of the folded and active state of CFTR depends on a diversity of molecular features from individual amino acids to domain-domain interactions. Identifying and understanding such elements, both in the cell membrane and when isolated and purified from the cell membrane, is key to understanding pathogenesis at the molecular level and therefore to provide rational therapeutic routes. The most recent advances in stability assessment, CFTR sequence design to enhance stability, and structure determination of CFTR will be presented.
Describe the 3D structure of CFTR and its functional and therapeutic value to CF.
Identify critical molecular features within CFTR that influence the stability of the protein in vivo and in vitro.
Demonstrate the importance of mechanism-based assessment of rare CFTR alleles to identify possible therapeutic intervention for patients with rare forms of CF.