《PNAS,6月5日,Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-bonding and hydrophobic interactions》

  • 来源专题:COVID-19科研动态监测
  • 编译者: xuwenwhlib
  • 发布时间:2020-06-07
  • Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-bonding and hydrophobic interactions

    View ORCID ProfileYingjie Wang, Meiyi Liu, and View ORCID ProfileJiali Gao

    PNAS first published June 5, 2020 https://doi.org/10.1073/pnas.2008209117

    Edited by Peter J. Rossky, Rice University, Houston, TX, and approved May 27, 2020 (received for review April 27, 2020)

    Abstract

    Molecular dynamics and free energy simulations have been carried out to elucidate the structural origin of differential protein–protein interactions between the common receptor protein angiotensin converting enzyme 2 (ACE2) and the receptor binding domains of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) [A. E. Gorbalenya et al., Nat. Microbiol. 5, 536–544 (2020)] that causes coronavirus disease 2019 (COVID-19) [P. Zhou et al., Nature 579, 270–273 (2020)] and the SARS coronavirus in the 2002–2003 (SARS-CoV) [T. Kuiken et al., Lancet 362, 263–270 (2003)] outbreak. Analysis of the dynamic trajectories reveals that the binding interface consists of a primarily hydrophobic region and a delicate hydrogen-bonding network in the 2019 novel coronavirus. A key mutation from a hydrophobic residue in the SARS-CoV sequence to Lys417 in SARS-CoV-2 creates a salt bridge across the central hydrophobic contact region, which along with polar residue mutations results in greater electrostatic complementarity than that of the SARS-CoV complex. Furthermore, both electrostatic effects and enhanced hydrophobic packing due to removal of four out of five proline residues in a short 12-residue loop lead to conformation shift toward a more tilted binding groove in the complex in comparison with the SARS-CoV complex. On the other hand, hydrophobic contacts in the complex of the SARS-CoV–neutralizing antibody 80R are disrupted in the SARS-CoV-2 homology complex model, which is attributed to failure of recognition of SARS-CoV-2 by 80R.

  • 原文来源:https://www.pnas.org/content/early/2020/06/04/2008209117
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  • 《PNAS,5月6日,Cell entry mechanisms of SARS-CoV-2》

    • 来源专题:COVID-19科研动态监测
    • 编译者:xuwenwhlib
    • 发布时间:2020-05-07
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  • 《6月5日_深圳湾实验室等研究称通过氢键和疏水作用的网络增强了SARS-CoV-2的受体结合》

    • 来源专题:COVID-19科研动态监测
    • 编译者:zhangmin
    • 发布时间:2020-06-07
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