{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Gupta M"],"funding":["NIBIB NIH HHS","NCRR NIH HHS","NIA NIH HHS","NIAID NIH HHS","NIMH NIH HHS","NCI NIH HHS","NIGMS NIH HHS","NIH HHS"],"pubmed_abstract":["The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIG"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2021.05.10.443524"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8132225"],"repository":["biostudies-literature"],"pubmed_title":["CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes."],"pmcid":["PMC8132225"],"funding_grant_id":["K99 MH119591","S10 RR026814","F32 GM133129","U19 AI135990","R01 GM024485","T32 EB009383","U19 AI135972","R37 GM024485","S10 OD026881","F32 CA239333","R35 GM118099","T32 GM007618","R01 AI128214","K99 GM138753","P50 AI150476","P01 AI063302","K99 AG070271","S10 OD020054","F30 CA247147","R01 AI143292","R01 AI120694","F32 GM133084","P01 AI095208","S10 OD021741","F32 GM137463"],"pubmed_authors":["Zhang K","Fraser JS","Wang F","Lopez KE","Frost A","Thwin AC","Hernandez E","Sun M","Pelin A","Remesh SG","Billesbolle C","Safari M","Diwanji D","Doan L","Jin M","Peters JK","Diallo A","Gupta M","Linossi E","Tse E","Owens TW","Verba KA","Krogan NJ","Li J","Chen J","Jang G","Li F","Li YL","Li Y","Puchades C","Chen KH","Lo M","Moritz M","Moss FR","Southworth DR","Azumaya CM","Titus EW","Fossati A","Smith AM","Schaefer K","Zuliani-Alvarez L","Young ID","Tsui TKM","QCRG Structural Biology Consortium","Kratochvil HT","Chio US","Kim K","Nowotny C","Pospiech TH","Rosenberg OS","Cheng Y","Bouhaddou M","Liu Y","Lopez J","Pawar KI","Rizo AN","Paul MD","Tabios MC","Asarnow D","Manglik A","Zhou F","Yu Z","Nguyen HC","Zhao J","Campbell MG","Jura N","Lam VL","Merz GE","Stroud RM","Herrera N","Zhou Y","Kortemme T","Dickinson MS","Zhang Y","Swaney DL","Brilot AF","Schulze-Gahmen U","Agard DA","Pourmal S","Trenker R","Mancino A"],"additional_accession":[]},"is_claimable":false,"name":"CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.","description":"The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIG","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2026-04-08T07:58:30.163Z","creation":"2025-05-18T11:27:49.261Z"},"accession":"S-EPMC8132225","cross_references":{"pubmed":["34013269"],"doi":["10.1101/2021.05.10.443524"]}}