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

作     者：Hui Yu,Xi Zhao*,Xian-li Feng,Xu-ri Huang State Key Laboratory of Theoretical and Computational Chemistry,Institute of Theoretical Chemistry,Jilin University,Changchun,130023,People''s Republic of China 

会议名称：《中国化学会第28届学术年会》

会议日期：2012年

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学] 

摘      要：Pheromone-binding proteins （PBP） transport hydrophobic pheromones through the aqueous medium to their *** 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 ***,so far the mechanism of MOP-release from the protein is ***,in this contribution the process and pathway of the MOP-release from CquiOBP1 are determined by conventional MD,essential dynamics and essential dynamics *** detailed analysis of the release process suggests the intrinsic flexibility of MOP,the distribution of contacts with MOP and local conformational changes of CquiOBP1 are crucial.