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Structure-based design of a SARS-CoV-2 Omicron-specific inhibitor


ABSTRACT:

SUBMITTER: Axel T Brunger 

PROVIDER: EMPIAR-11476 | biostudies-other |

REPOSITORIES: biostudies-other

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Structure-based design of a SARS-CoV-2 Omicron-specific inhibitor.

Yang Kailu K   Wang Chuchu C   Kreutzberger Alex J B AJB   White K Ian KI   Pfuetzner Richard A RA   Esquivies Luis L   Kirchhausen Tomas T   Brunger Axel T AT  

Proceedings of the National Academy of Sciences of the United States of America 20230320 13


The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) introduced a relatively large number of mutations, including three mutations in the highly conserved heptad repeat 1 (HR1) region of the spike glycoprotein (S) critical for its membrane fusion activity. We show that one of these mutations, N969K induces a substantial displacement in the structure of the heptad repeat 2 (HR2) backbone in the HR1HR2 postfusion bundle. Due to this mutation, fusion-entry peptide inhi  ...[more]

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