Structural insights into the ligand binding and releasing mechanism of Antheraea polyphemus pheromone-binding protein 1: role of the C-terminal tail.

ABSTRACT: Pheromone-binding proteins (PBPs) in lepidopteran moths selectively transport the hydrophobic pheromone molecules across the sensillar lymph to trigger the neuronal response. Moth PBPs are known to bind ligand at physiological pH and release it at acidic pH while undergoing a conformational change. Two molecular switches are considered to play a role in this mechanism: (i) protonation of His(70) and His(95) situated at one end of binding pocket and (ii) switch of the unstructured C-terminus at the other end of the binding pocket to a helix that enters the pocket. We have reported previously the role of the histidine-driven switch in ligand release for Antheraea polyphemus PBP1 (ApolPBP1). Here we show that the C-terminus plays a role in the ligand release and binding mechanism of ApolPBP1.

SUBMITTER: Katre UV 

PROVIDER: S-EPMC3571721 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature