Fig. 2.
Binding of bombykol to BmorPBP mutated by replacing one or two of the three acidic residues at the C-terminus with the corresponding amide residues. Binding of bombykol to (A) double mutated and (B) one-point mutations compared to the native protein.
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Effect of the N-terminus on binding at low pH
The N-terminus (from 1-Ser to 8-Leu) of BmorPBP forms a α-helix at high Doxazosin Mesylate [15] which unfolds at low pH [10]. To test whether the N-terminus is involved in binding and/or release of pheromone, we compared binding of the N-terminus truncated BmorPBP, Δ1S-8LBmorPBP, with binding of BmorPBP to bombykol. Δ1S-8LBmorPBP resembled the intact BmorPBP in that it binds to bombykol at high, but not at low pH (Fig. 3A) thus suggesting that the N-terminus may not be involved in binding and/or release of bombykol.
Fig. 3.
Binding of bombykol to BmorPBP (A) truncated at the N-terminus or (B) having one of the three histidines, His-69, His-70, and His-95, associated with a lid of the binding cavity, replaced by alanine.
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