What a twist: structural biology of the SARS-CoV-2 helicase nsp13

• DOI: 10.1080/0889311x.2024.2309494
• Publication Date: 2024-02-27T07:38:15Z
• Authors: Sam Horrell; Sam Martino; Ferdinand Kirsten; Dénes Berta; Gianluca Santoni; Andrea Thorn
• Keywords: helicase; SARS-CoV-2; structure based drug design; COVID-19; structural biology

SARS-CoV-2 nsp13 is a multifunctional helicase from superfamily 1B. It unwinds the viral RNA genome for replication and thought to play role in 5' mRNA capping produce mature using its triphosphatase activity. The sequence structure are highly conserved nidovirales protein essential infection cycle, acting as standalone enzyme conjunction with other proteins, making promising target structure-based drug design. By inhibiting activity, phosphatase or interaction RNA-dependent polymerase we could interrupt replication. A total of 72 structures have been published databank (PDB) date, 56 monomers 16 part complex. made up five folds, N- C-terminus, zinc-binding domain, stalk beta barrel domain 1B, RecA-like subdomain 1A, This review summarizes current structural functional knowledge surrounding related helicases, well design efforts complementary provide downstream users solid foundation better inform their work.