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分子模拟研究南方家蚊气味结合蛋白中配体释放的机制。

Molecular simulations study of ligand-release mechanism in an odorant-binding protein from the southern house mosquito.

机构信息

State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023, P.R. China.

出版信息

J Biomol Struct Dyn. 2013;31(5):485-94. doi: 10.1080/07391102.2012.706069. Epub 2012 Aug 13.

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.

摘要

信息素结合蛋白通过水相将疏水性信息素转运至其受体。Culex quinquefasciatus 的气味结合蛋白 (OBP) (CquiOBP1) 与一种产卵信息素 (5R,6S)-6-乙酰氧基-5-十六烷醇 (MOP) 结合,在感应产卵线索方面发挥着关键作用。然而,到目前为止,MOP 从蛋白质中释放的机制尚不清楚。因此,在本研究中,通过传统分子动力学、本征动力学 (ED) 和 ED 采样确定了 MOP 从 CquiOBP1 中释放的过程和途径。释放过程的详细分析表明 MOP 的固有灵活性、与 MOP 的接触分布以及 CquiOBP1 的局部构象变化至关重要。

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