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[Preprint]. 2020 Oct 7:2020.10.07.307546. [Version 1] 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, Kristoper Nolte, Alex Payne, Matthew G Reeves, Jane Richardson, Gianluca Santoni, Sabrina Stäb, Dale Tronrud, Christopher Williams, Andrea Thorn
PMCID: PMC7553165  PMID: 33052340

Abstract

During the COVID-19 pandemic, structural biologists have 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 200 structures from SARS-CoV previously solved, 367 structures covering 16 of the viral proteins have been released in the span of only 6 months.

These structural models serve as basis for research worldwide 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 are even more common among these structures, which were solved under immense pressure.

From the beginning of the pandemic, the Coronavirus Structural Taskforce has categorized, evaluated and reviewed all of these experimental protein structures in order to help downstream users and original authors. Our website also offers improved models for many key structures, which have been used by Folding@Home, OpenPandemics, the EU JEDI COVID-19 challenge, and others. Here, we describe our work for the first time, give an overview of common problems, and describe a few of these structures that have since acquired better versions in the worldwide Protein Data Bank, either from new data or as depositor re-versions using our suggested changes.

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