title: Exploring the membrane fusion mechanism through force-induced disassembly of HIV-1 six-helix bundle.
abstract: Enveloped virus, such as HIV-1, employs membrane fusion mechanism to invade into host cell. HIV-1 gp41 ectodomain uses six-helix bundle configuration to accomplish this process. Using molecular dynamic simulations, we confirmed the stability of this six-helix bundle by showing high occupancy of hydrogen bonds and hydrophobic interactions. Key residues and interactions important for the bundle integration were characterized by force-induced unfolding simulations of six-helix bundle, exhibiting the collapse order of these groups of interactions. Moreover, our results in some way concerted with a previous theory that the formation of coiled-coil choose a route which involved cooperative interactions between the N-terminal and C-terminal helix.
authors.affiliation: Key Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Beijing Key Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
authors.forename: Kai
authors.initials: K
authors.lastname: Gao
authors.affiliation: Key Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Beijing Key Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: Key Laboratory of RNA Biology, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; Beijing Key Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. Electronic address: jlou@ibp.ac.cn.
authors.forename: Jizhong
authors.initials: J
authors.lastname: Lou
mesh_terms: D003198:Computer Simulation; D015700:HIV Envelope Protein gp41 / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure*; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D040542:Mechanotransduction, Cellular / Q000502:physiology; D008560:Membrane Fluidity / Q000502:physiology; D008561:Membrane Fusion / Q000502:physiology*; D008846:Micromanipulation / Q000379:methods; D008954:Models, Biological; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D017510:Protein Folding; D021122:Protein Subunits; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship
chemical_list: D015700:HIV Envelope Protein gp41; D021122:Protein Subunits; C514787:gp41 protein, Human immunodeficiency virus 1
keywords: Interfacial interaction; Membrane fusion; Molecular dynamics simulations; Protein unfolding; Six-helix bundle