TY  - JOUR
KW  - SARS-CoV-2; COVID-19;helicase; structural biology;structure based drug design
IS  - 4
SN  - 0889-311X
ID  - discovery10190181
VL  - 29
N2  - SARS-CoV-2 nsp13 is a multifunctional helicase from helicase superfamily 1B. It unwinds the viral RNA genome for replication and is thought to play a role in 5? mRNA capping to produce mature mRNA using its triphosphatase activity. The sequence and structure are highly conserved in nidovirales and the protein is essential to the viral infection cycle, acting as a standalone enzyme and in conjunction with other SARS-CoV-2 proteins, making SARS-CoV-2 helicase a promising target for structure-based drug design. By inhibiting helicase activity, phosphatase activity, or its interaction with the RNA-dependent RNA polymerase we could interrupt viral replication. A total of 72 structures of SARS-CoV-2 nsp13 have been published in the protein databank (PDB) to date, 56 monomers and 16 as part of a complex. The structure of nsp13 is made up of five conserved folds, from N- to C-terminus, a zinc-binding domain, stalk domain, beta barrel domain 1B, RecA-like subdomain 1A, and RecA-like subdomain 1B. This review summarizes the current structural and functional knowledge surrounding SARS-CoV-2 nsp13 and related helicases, as well as the structure-based drug design efforts to date, and other complementary knowledge to provide downstream users of SARS-CoV-2 structures with a solid foundation to better inform their work.
AV  - public
EP  - 227
Y1  - 2024/02/26/
UR  - https://doi.org/10.1080/0889311X.2024.2309494
A1  - Horrell, Sam
A1  - Martino, Sam
A1  - Kirsten, Ferdinand
A1  - Berta, Denes
A1  - Santoni, Gianluca
A1  - Thorn, Andrea
SP  - 202
N1  - This version is the author accepted manuscript. For information on re-use, please refer to the publisher?s terms and conditions.
TI  - What a twist: structural biology of the SARS-CoV-2 helicase nsp13
PB  - Taylor & Francis
JF  - Crystallography Reviews
ER  -