Article
Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor.
Biophysical journal - 1 Jul 2005
Wang Ying, Xu Le, Pasek Daniel A, Gillespie Dirk, Meissner Gerhard
Abstract excerpt
Sequence comparison suggests that the ryanodine receptors (RyRs) have pore architecture similar to that of the bacterial K+ channel KcsA. The lumenal loop linking the two most C-terminal transmembrane spanning segments in the RyRs has a predicted pore helix and an amino acid motif (GGGIG) similar to the selectivity filter (TVGYG) of KcsA identified by x-ray analysis. The RyRs have many negatively charged amino...
Topics
- Amino Acid Motifs
- Amino Acid Sequence
- Amino Acids
- Animals
- Aspartic Acid
- Calcium
- Cations
- Cell Line
- DNA, Complementary
- Genetic Vectors
- Glutamic Acid
- Humans
- Immunoblotting
- Ions