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10.1107/S2053230X20011814

http://scihub22266oqcxt.onion/10.1107/S2053230X20011814
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33006576!7531248!33006576
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suck abstract from ncbi


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pmid33006576      Acta+Crystallogr+F+Struct+Biol+Commun 2020 ; 76 (Pt 10): 483-487
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  • Room-temperature neutron and X-ray data collection of 3CL M(pro) from SARS-CoV-2 #MMPMID33006576
  • Kneller DW; Phillips G; Kovalevsky A; Coates L
  • Acta Crystallogr F Struct Biol Commun 2020[Oct]; 76 (Pt 10): 483-487 PMID33006576show ga
  • 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).
  • |Betacoronavirus/chemistry/*enzymology/genetics[MESH]
  • |COVID-19[MESH]
  • |Catalytic Domain[MESH]
  • |Coronavirus 3C Proteases[MESH]
  • |Coronavirus Infections/*virology[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Cysteine Endopeptidases/*chemistry/genetics[MESH]
  • |Humans[MESH]
  • |Models, Molecular[MESH]
  • |Neutron Diffraction[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/*virology[MESH]
  • |Protein Conformation[MESH]
  • |Recombinant Proteins/chemistry/genetics[MESH]
  • |SARS-CoV-2[MESH]
  • |Temperature[MESH]


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