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Figure 6.
Figure 6. Connolly surface of the lowest energy structure
of holo Bet v 4 colored according to hydrophobicity (top;
backbone yellow, hydrophobic residues green, hydrophilic
residues blue) or electrostatic potential (bottom; negative
potential red, positive potential blue). Opposite view as in
Figure 4 and Figure 5. The electric charge of the side-chain of
His48 depends on pH, at pH 6.0 it is predominantly protonated.
The COOH-terminal helix a[5] does not cover the hydrophobic
groove lined by negatively charged residues completely.
Formation of the domain-swapped dimer of holo Phl p 7 closes
this hydrophobic groove, resulting in a hydrophobic cavity which
is no longer solvent-accessible.[26.] The Figure was prepared
with InsightII 98.0 (Molecular Simulations Inc., San Diego, CA,
USA) and GRASP 1.2. [94.]
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