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[Preprint]. 2020 Dec 28:2020.10.07.307546. Originally published 2020 Oct 7. [Version 2] doi: 10.1101/2020.10.07.307546

Making the invisible enemy visible

Tristan Croll, Kay Diederichs, Florens Fischer, Cameron Fyfe, Yunyun Gao, Sam Horrell, Agnel Praveen Joseph, Luise Kandler, Oliver Kippes, Ferdinand Kirsten, Konstantin Müller, Kristopher Nolte, Alexander Payne, Matthew G Reeves, Jane Richardson, Gianluca Santoni, Sabrina Stäb, Dale Tronrud, Lea von Soosten, Christopher Williams, Andrea Thorn
PMCID: PMC7553165  PMID: 33052340

Abstract

During the COVID-19 pandemic, structural biologists rushed to solve the structures of the 28 proteins encoded by the SARS-CoV-2 genome in order to understand the viral life cycle and enable structure-based drug design. In addition to the 204 previously solved structures from SARS-CoV-1, 548 structures covering 16 of the SARS-CoV-2 viral proteins have been released in a span of only 6 months. These structural models serve as the basis for research to understand how the virus hijacks human cells, for structure-based drug design, and to aid in the development of vaccines. However, errors often occur in even the most careful structure determination - and may be even more common among these structures, which were solved quickly and under immense pressure. The Coronavirus Structural Task Force has responded to this challenge by rapidly categorizing, evaluating and reviewing all of these experimental protein structures in order to help downstream users and original authors. In addition, the Task Force provided improved models for key structures online, which have been used by Folding@Home, OpenPandemics, the EU JEDI COVID-19 challenge and others.

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