Article
Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating.
The Journal of clinical investigation - 1 Feb 2003
Shen Xin-Ming, Ohno Kinji, Tsujino Akira, Brengman Joan M, Gingold Monique, Sine Steven M, Engel Andrew G
Abstract excerpt
We describe a highly disabling congenital myasthenic syndrome (CMS) associated with rapidly decaying, low-amplitude synaptic currents, and trace its cause to a valine to leucine mutation in the signature cystine loop (cys-loop) of the AChR alpha subunit. The recently solved crystal structure of an ACh-binding protein places the cys-loop at the junction between the extracellular ligand-binding and transmembrane...
Topics
- Acetylcholine
- Amino Acid Sequence
- Case-Control Studies
- Cell Line
- Child, Preschool
- Cysteine
- Female
- Humans
- In Vitro Techniques
- Ion Channel Gating
- Kinetics
- Male
- Models, Molecular
- Molecular Sequence Data