6WQF

Structural Plasticity of the SARS-CoV-2 3CL Mpro Active Site Cavity Revealed by Room Temperature X-ray Crystallography

6WQF の概要

• エントリーDOI: 10.2210/pdb6wqf/pdb
• 分子名称: 3C-like proteinase (2 entities in total)
• 機能のキーワード: sars-cov-2 main protease, viral protein, hydrolase
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33825.55

構造登録者

Kneller, D.W.,Kovalevsky, A.,Coates, L. (登録日: 2020-04-28, 公開日: 2020-05-06, 最終更新日: 2023-10-18)

主引用文献

Kneller, D.W.,Phillips, G.,O'Neill, H.M.,Jedrzejczak, R.,Stols, L.,Langan, P.,Joachimiak, A.,Coates, L.,Kovalevsky, A.
Structural plasticity of SARS-CoV-2 3CL Mproactive site cavity revealed by room temperature X-ray crystallography.
Nat Commun, 11:3202-3202, 2020

PubMed Abstract: The COVID-19 disease caused by the SARS-CoV-2 coronavirus has become a pandemic health crisis. An attractive target for antiviral inhibitors is the main protease 3CL M due to its essential role in processing the polyproteins translated from viral RNA. Here we report the room temperature X-ray structure of unliganded SARS-CoV-2 3CL M, revealing the ligand-free structure of the active site and the conformation of the catalytic site cavity at near-physiological temperature. Comparison with previously reported low-temperature ligand-free and inhibitor-bound structures suggest that the room temperature structure may provide more relevant information at physiological temperatures for aiding in molecular docking studies.

PubMed: 32581217
DOI: 10.1038/s41467-020-16954-7

実験手法

X-RAY DIFFRACTION (2.3 Å)