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Arginine 2510 is on the exposed highly conserved face of the dimerisation helix (Fig. 5A) and makes salt bridges to neighbouring residues.
As is readily apparent in this new figure (Additional file 4), when only the more reliable PTMs are considered, there remains an almost two-fold enhancement of post-translationally modified residues on the variable face (conserved face: 16 modified residues; variable face: 31 modified residues).
Residues at positions 330 and 407 cluster away from the hydrophobic trough and residue 121 occurs on the more conserved face of the molecule.
The "variable face" has a total of 37 modified residues, compared with just 19 such residues seen on the "conserved face" of the protein – an almost two-fold increase.
Taking into consideration residues that can be alternatively modified the "conserved face" displays 28 possible modifications amongst 19 residues, while the "variable face" supports a total of 53 modifications.
From the number-counts there is an almost two-fold increase in modifications on the variable face of the protein (19 on the conserved face; 37 on the variable face).
Similar(52)
Both receptors contain a highly conserved hydrophobic face in TM6, but they differ in one important position, where drd2 has a histidine and drd1 an asparagine residue, the latter being conserved with the template structure.
In other words, greater neural processing resources are directed toward threat stimuli and processing resources are conserved when facing a nonthreat stimulus situation.
This finding suggests that rather than expending more effort in general, elite warfighters show more focused neural and performance tuning, such that greater neural processing resources are directed toward threat stimuli and processing resources are conserved when facing a nonthreat stimulus situation.
Hsp104 contains conserved, channel-facing tyrosine residues in both NBDs, and mutation of the one in NBD2 significantly reduces thermotolerance (Lum et al., 2004).
Mapping the conserved residues of mouse laminin α-chains onto the α5LN domain structure showed that the β6 β3 β8 face of the β-sandwich is more highly conserved than the opposite face (not shown).
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