CFTR 14-3-3 and R Domain

5D3F

The R domain is in pink and the 14-3-3 domains are in green and blue.

At 2.74 Å the structure of 14-3-3 protein bound to CFTR regulatory R domain
has been found to enhance CFTR trafficking to the plasma membrane. Fusicoccin-A, a natural-product tool compound used in studies of 14-3-3 biology, can stabilize the interaction between 14-3-3 and CFTR by selectively interacting with a secondary binding motif of CFTR (pS753).

Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. Proceedings of the National Academy of Sciences of the United States of America

(PubMed)

5D3F (PDB)

 CFTR hNBD1 (Nucleotide Binding Domain 1) with Phe508 Cartoon View

2BBO

The alpha helices in pink and beta sheets shown in yellow make up the secondary structures. Regions that are without secondary structures are white.


The ΔF508 mutation in nucleotide-binding domain 1 (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR) is the predominant cause of cystic fibrosis. biophysical studies on human F508 and ΔF508 domains showed only local structural changes restricted to residues 509–511 and only minor differences in folding rate and stability.

Structure and Dynamics of NBD1 from CFTR Characterized Using Crystallography and Hydrogen/Deuterium Exchange Mass Spectrometry

(PubMed)

2BBO (PDB)
Next page