Contents
29 September 2020
Vol 13, Issue 651
Vol 13, Issue 651
Research Articles
- High-resolution structures of the SARS-CoV-2 2′-O-methyltransferase reveal strategies for structure-based inhibitor design
Crystal structures of an mRNA-capping enzyme from SARS-CoV-2 in complex with its substrates suggest targets for drug design.
- The purinergic receptor P2Y11 choreographs the polarization, mitochondrial metabolism, and migration of T lymphocytes
Relocalization of P2Y11 purinergic receptors enables the polarization needed for T cell migration.
Editors' Choice
- Microbial metabolite protects against infection
Commensal-derived d-lactate promotes pathogen capture and clearance by Kupffer cells in the liver.
About The Cover
Online Cover This week features a Research Article that reports several crystal structures of a SARS-CoV-2 methyltransferase that is critical for mRNA capping in complex with various combinations of its methyl donor and cap structure substrates, a reaction product, and an inhibitor. The image shows the two subunits of the methyltransferase in complex with the methyl donor SAM (green) and two Zn2+ ions (purple). [Image: Rosas-Lemus et al./Science Signaling]
