Structural Basis for OAS2 Regulation and its Antiviral Function
Structural Basis for OAS2 Regulation and its Antiviral Function
About this item
Full title
Author / Creator
Merold, Veronika , Bekere, Indra , Kretschmer, Stefanie , Schnell, Adrian F , Kmiec, Dorota , Sivarajan, Rinu , Lammens, Katja , Liu, Rou , Mergner, Julia , Teppert, Julia , Hirschenberger, Maximilian , Hammes, Sarah , Buder, Kathrin , Weitz, Marcus , Koenig, Lars M , Pichlmair, Andreas , Schwierz, Nadine , Sparrer, Konstantin Mj , Lee-Kirsch, Min Ae and Carina C De Oliveira Mann
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Journal title
Language
English
Formats
Publication information
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Subjects
More information
Scope and Contents
Contents
Oligoadenylate synthetase (OAS) proteins are immune sensors for double-stranded RNA and critical for restricting viruses. OAS2 comprises two OAS domains, only one of which can synthesize 2'-5'-oligoadenylates for RNase L activation. Existing structures of OAS1 provide a model for enzyme activation, but do not explain how multiple OAS domains discri...
Alternative Titles
Full title
Structural Basis for OAS2 Regulation and its Antiviral Function
Authors, Artists and Contributors
Author / Creator
Bekere, Indra
Kretschmer, Stefanie
Schnell, Adrian F
Kmiec, Dorota
Sivarajan, Rinu
Lammens, Katja
Liu, Rou
Mergner, Julia
Teppert, Julia
Hirschenberger, Maximilian
Hammes, Sarah
Buder, Kathrin
Weitz, Marcus
Koenig, Lars M
Pichlmair, Andreas
Schwierz, Nadine
Sparrer, Konstantin Mj
Lee-Kirsch, Min Ae
Carina C De Oliveira Mann
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_biorxiv_primary_2025_01_28_635220
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_biorxiv_primary_2025_01_28_635220
Other Identifiers
ISSN
2692-8205
E-ISSN
2692-8205
DOI
10.1101/2025.01.28.635220
