Browsing by Author "Hou, Guangjin"
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Item Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site(Nature Publishing Group, 2016-03-04) Liu, Chuang; Perilla, Juan R.; Ning, Jiying; Lu, Manman; Hou, Guangjin; Ramalho, Ruben; Himes, Benjamin A.; Zhao, Gongpu; Bedwell, Gregory J.; Byeon, In-Ja; Ahn, Jinwoo; Gronenborn, Angela M.; Prevelige, Peter E.; Rousso, Itay; Aiken, Christopher; Polenova, Tatyana; Schulten, Klaus; Zhang, Peijun; Chuang Liu, Juan R. Perilla, Jiying Ning, Manman Lu, Guangjin Hou, Ruben Ramalho, Benjamin A. Himes, Gongpu Zhao, Gregory J. Bedwell, In-Ja Byeon, Jinwoo Ahn, Angela M. Gronenborn, Peter E. Prevelige, Itay Rousso, Christopher Aiken, Tatyana Polenova, Klaus Schulten & Peijun Zhang; Lu, Manman; Hou, Guangjin; Polenova, TatyanaThe host cell factor cyclophilin A (CypA) interacts directly with the HIV-1 capsid and regulates viral infectivity. Although the crystal structure of CypA in complex with the N-terminal domain of the HIV-1 capsid protein (CA) has been known for nearly two decades, how CypA interacts with the viral capsid and modulates HIV-1 infectivity remains unclear. We determined the cryoEM structure of CypA in complex with the assembled HIV-1 capsid at 8-Å resolution. The structure exhibits a distinct CypA-binding pattern in which CypA selectively bridges the two CA hexamers along the direction of highest curvature. EM-guided all-atom molecular dynamics simulations and solid-state NMR further reveal that the CypA-binding pattern is achieved by single-CypA molecules simultaneously interacting with two CA subunits, in different hexamers, through a previously uncharacterized non-canonical interface. These results provide new insights into how CypA stabilizes the HIV-1 capsid and is recruited to facilitate HIV-1 infection.Item Evolution of multiple spillover hydrogen species on anatase titanium dioxide(Cell Reports Physical Science, 2022-12-21) Liu, Kairui; Hou, Guangjin; Gao, Pan; Nie, Xuezhong; Bai, Shi; Janik, Michael J.; Zhang, Z. ConradHydrogen spillover is a widespread phenomenon on reducible metal oxide surfaces, with numerous observations confirming its occurrence. However, direct physical characterization of the spillover hydrogen species on an oxide catalyst support remains challenging. Differentiating the binding sites of specific spillover hydrogen species has been elusive. Herein, we vary temperature and reductive conditions, then quench and detect the physicochemical character of three distinct spillover hydrogen species on anatase titanium dioxide (TiO2-A) by deuterium magic-angle-spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy, aided by density functional theory. Fast cooling during the sample preparation is crucial in quenching the spillover deuterium species to enable MAS NMR detection. Energetically favorable spillover deuterium species evolve from deuteron to deuteride states with increasing reduction temperature. Prevailing deuteron species reside on the 2-fold-coordinated O2c site of the TiO2-A (101) surface at low reduction temperature. At high reduction temperature, deuterides residing at oxygen vacancies (Ti6c–D–Ti5c) are formed.