PropertyValue
?:abstract
  • The replication of SARS-CoV-2 produces two large polyproteins, pp1a and pp1ab, that are inactive until cleavage by the viral chymotrypsin-like cysteine protease enzyme (3CL M(pro)) into a series of smaller functional proteins At the heart of 3CL M(pro) is an unusual catalytic dyad formed by the side chains of His41 and Cys145 and a coordinated water molecule The catalytic mechanism by which the enzyme operates is still unknown, as crucial information on the protonation states within the active site is unclear To experimentally determine the protonation states of the catalytic site and of the other residues in the substrate-binding cavity, and to visualize the hydrogen-bonding networks throughout the enzyme, room-temperature neutron and X-ray data were collected from a large H/D-exchanged crystal of ligand-free (apo) 3CL M(pro)
is ?:annotates of
?:creator
?:journal
  • Acta_Crystallogr_F_Struct_Biol_Commun
?:license
  • unk
?:publication_isRelatedTo_Disease
?:source
  • WHO
?:title
  • Room-temperature neutron and X-ray data collection of 3CL M(pro) from SARS-CoV-2
?:type
?:who_covidence_id
  • #811055
?:year
  • 2020

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