Discovering critical residues in glutathione reductase - Gentoo

Figure 10: Structural stabilization. See text for discussion.
The final group of conserved residues in this analysis falls at a junction of
beta sheets and an alpha helix (Figure 10). Positively charged His434 and
Lys420 extend out from the beta sheets toward the helix's Asp227 and Glu384
from the nearby loop. These 100% conserved, balanced charges suggest some
gain in structural stability. It may be that this particular part of the structure,
while nowhere near the active site, must be retained or some sort of allosteric
effect could reach into the active site and dramatically affect binding or
catalysis. Another possibility is that these residues are critical in GR's folding
process.
In conclusion, this study has used bioinformatics as a tool in analysis of
structure-function relationships. Remaining work includes checking whether the