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PubMed:33060199 JSONTXT 40 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-100 Sentence denotes Unusual zwitterionic catalytic site of SARS-CoV-2 main protease revealed by neutron crystallography.
T2 101-227 Sentence denotes The main protease (3CL Mpro) from SARS-CoV-2, the etiological agent of COVID-19, is an essential enzyme for viral replication.
T3 228-311 Sentence denotes 3CL Mpro possesses an unusual catalytic dyad composed of Cys145 and His41 residues.
T4 312-603 Sentence denotes A critical question in the field has been what the protonation states of the ionizable residues in the substrate-binding active site cavity are; resolving this point would help understand the catalytic details of the enzyme and inform rational drug development against this pernicious virus.
T5 604-782 Sentence denotes Here, we present the room-temperature neutron structure of 3CL Mpro, which allowed direct determination of hydrogen atom positions and, hence, protonation states in the protease.
T6 783-1034 Sentence denotes We observe that the catalytic site natively adopts a zwitterionic reactive form where Cys145 is in the negatively charged thiolate state, and His41 is doubly protonated and positively charged, instead of the neutral unreactive state usually envisaged.
T7 1035-1261 Sentence denotes The neutron structure also identified the protonation states, and thus electrical charges, of all other amino acid residues and revealed intricate hydrogen bonding networks in the active site cavity and at the dimer interface.
T8 1262-1523 Sentence denotes The fine atomic details present in this structure were made possible by the unique scattering properties of the neutron, which is an ideal probe for locating hydrogen positions and experimentally determining protonation states at near-physiological temperature.
T9 1524-1707 Sentence denotes Our observations provide critical information for structure-assisted and computational drug design, allowing precise tailoring of inhibitors to the enzyme's electrostatic environment.