AI Article Synopsis
- Pheromone-binding proteins transport hydrophobic pheromones to their receptors, crucial for sensing oviposition cues.
- The study focuses on the odorant-binding protein CquiOBP1 from Culex quinquefasciatus, which binds to the oviposition pheromone MOP.
- Research using molecular dynamics analyzes how MOP is released from CquiOBP1, highlighting the importance of MOP's flexibility and the protein's conformational changes during the release process.
Article Abstract
Pheromone-binding proteins transport hydrophobic pheromones through the aqueous medium to their receptors. The odorant-binding protein (OBP) of Culex quinquefasciatus (CquiOBP1), which binds to an oviposition pheromone (5R,6S)-6-acetoxy-5-hexadecanolide (MOP), plays a key role in sensing oviposition cues. However, so far the mechanism of MOP release from the protein is unclear. Therefore, in this contribution the process and pathway of the MOP release from CquiOBP1 are determined by conventional molecular dynamics, essential dynamics (ED), and ED sampling. The detailed analysis of the release process suggests the intrinsic flexibility of MOP, the distribution of contacts with MOP and local conformational changes of CquiOBP1 is crucial.
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| http://dx.doi.org/10.1080/07391102.2012.706069 | DOI Listing |
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