Article
Two positively charged amino acid side-chains in the inner vestibule of the CFTR channel pore play analogous roles in controlling anion binding and anion conductance.
Cellular and molecular life sciences : CMLS - 1 Jun 2021
Linsdell Paul, Irving Christina L, Cowley Elizabeth A, El Hiani Yassine
Abstract excerpt
Positively charged amino acid side-chains play important roles in anion binding and permeation through the CFTR chloride channel. One pore-lining lysine residue in particular (K95) has been shown to be indispensable for anion binding, conductance, and selectivity. Here, we use functional investigation of CFTR to show that a nearby arginine (R134) plays a functionally analogous role. Removal of this positive...
Topics
- Animals
- Anions
- Arginine
- Cells, Cultured
- Cricetinae
- Cystic Fibrosis Transmembrane Conductance Regulator
- Humans
- Lysine
- Mutation
- Patch-Clamp Techniques
- Protein Conformation