An Overview of the Crystallized Structures of the SARS-CoV-2

被引:38
作者
Ionescu, Mihaela Ileana [1 ,2 ]
机构
[1] Iuliu Hatieganu Univ Med & Pharm, Dept Microbiol, 6 Louis Pasteur, Cluj Napoca 400349, Romania
[2] Cty Emergency Clin Hosp, Dept Microbiol, Cluj Napoca 400006, Romania
关键词
COVID-19; Coronavirus; Spike; Inhibitors; Protein Data Bank; Molecular docking; ACUTE RESPIRATORY SYNDROME; CORONAVIRUS PAPAIN-LIKE; RNA-POLYMERASE; MERS-COV; TERMINAL DOMAIN; MOLECULAR-BASIS; SPIKE PROTEIN; SARS; INHIBITORS; RECEPTOR;
D O I
10.1007/s10930-020-09933-w
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Many research teams all over the world focus their research on the SARS-CoV-2, the new coronavirus that causes the so-called COVID-19 disease. Most of the studies identify the main protease or 3C-like protease (M-pro/3CL(pro)) as a valid target for large-spectrum inhibitors. Also, the interaction of the human receptor angiotensin-converting enzyme 2 (ACE2) with the viral surface glycoprotein (S) is studied in depth. Structural studies tried to identify the residues responsible for enhancement/weaken virus-ACE2 interactions or the cross-reactivity of the neutralizing antibodies. Although the understanding of the immune system and the hyper-inflammatory process in COVID-19 are crucial for managing the immediate and the long-term consequences of the disease, not many X-ray/NMR/cryo-EM crystals are available. In addition to 3CL(pro), the crystal structures of other nonstructural proteins offer valuable information for elucidating some aspects of the SARS-CoV-2 infection. Thus, the structural analysis of the SARS-CoV-2 is currently mainly focused on three directions-finding M-pro/3CL(pro) inhibitors, the virus-host cell invasion, and the virus-neutralizing antibody interaction.
引用
收藏
页码:600 / 618
页数:19
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