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Structural modeling of protein ensembles between E3 RING ligases and SARS-CoV-2: The role of zinc binding domains. | LitMetric

Structural modeling of protein ensembles between E3 RING ligases and SARS-CoV-2: The role of zinc binding domains.

J Trace Elem Med Biol

Department of Chemical, Physical, Mathematical and Natural Sciences, University of Sassari, Italy. Electronic address:

Published: January 2023

AI Article Synopsis

Article Abstract

Background: The ubiquitin system is a modification process with many different cellular functions including immune signaling and antiviral functions. E3 ubiquitin ligases are enzymes that recruit an E2 ubiquitin-conjugating enzyme bound to ubiquitin in order to catalyze the transfer of ubiquitin from the E2 to a protein substrate. The RING E3s, the most abundant type of ubiquitin ligases, are characterized by a zinc (II)-binding domain called RING (Really Interesting New Gene). Viral replication requires modifying and hijacking key cellular pathways within host cells such as cellular ubiquitination. There are well-established examples where a viral proteins bind to RING E3s, redirecting them to degrade otherwise long-lived host proteins or inhibiting E3's ubiquitination activity. Recently, three binary interactions between SARS-CoV-2 proteins and innate human immune signaling Ε3 RING ligases: NSP15-RNF41, ORF3a-TRIM59 and NSP9-MIB1 have been experimentally established.

Methods: In this work, we have investigated the mode of the previous experimentally supported NSP15-RNF41, ORF3a,-TRIM59 and NSP9-MIB1 binary interactions by in silico methodologies intending to provide structural insights of E3-virus interplay that can help identify potential inhibitors that could block SARS-CoV-2 infection of immune cells.

Conclusion: In silico methodologies have shown that the above human E3 ligases interact with viral partners through their Zn(II) binding domains. This RING mediated formation of stable SARS-CoV-2-E3 complexes indicates a critical structural role of RING domains in immune system disruption by SARS-CoV-2-infection.

Data Availability: The data used to support the findings of this research are included within the article and are labeled with references.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9531365PMC
http://dx.doi.org/10.1016/j.jtemb.2022.127089DOI Listing

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