  Energetically responsive residues of the 173 amino acid N-terminal domain of
the cardiac Ryanodine receptor RyR2 are identified by a simple elastic net
model. Residues that respond in a correlated way to fluctuations of spatially
neighboring residues specify a hydrogen bonded path through the protein. The
evolutionarily conserved residues of the protein are all located on this path
or in its close proximity. All of the residues of the path are either located
on the two Mir domains of the protein or are hydrogen bonded them. Two calcium
binding residues, E171 and E173, are proposed as potential binding region,
based on insights gained from the elastic net analysis of another calcium
channel receptor, the inositol 1,4,5-triphosphate receptor, IP3R. Analysis of
the disease causing A77V mutated RyR2 showed that the path is disrupted by the
loss of energy responsiveness of certain residues.
