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10.1021/acs.jpclett.1c00831 http://scihub22266oqcxt.onion/10.1021/acs.jpclett.1c00831 34110168!ä!34110168 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34110168&cmd=llinks): Failed to open stream: HTTP request failed! 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Conformational Dynamics in the Interaction of SARS-CoV-2 Papain-like Protease with Human Interferon-Stimulated Gene 15 Protein |pdf=|usr=}}{{34110168}} gab.com Text Conformational Dynamics in the Interaction of SARS-CoV-2 Papain-like Protease with Human Interferon-Stimulated Gene 15 Protein JO: J Phys Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=34110168 #FOAvip Papain-like protease (PLpro) from SARS-CoV-2 plays essential roles in the replication cycle of the virus. In particular, it preferentially interacts with and cleaves human interferon-stimulated gene 15 (hISG15) to suppress the innate immune response of the host. We used small-angle X-ray and neutron scattering combined with computational techniques to study the mechanism of interaction of SARS-CoV-2 PLpro with hISG15. We showed that hISG15 undergoes a transition from an extended to a compact state after binding to PLpro, a conformation that has not been previously observed in complexes of SARS-CoV-2 PLpro with ISG15 from other species. Furthermore, computational analysis showed significant conformational flexibility in the ISG15 N-terminal domain, suggesting that it is weakly bound to PLpro and supports a binding mechanism that is dominated by the C-terminal ISG15 domain. This study fundamentally improves our understanding of the SARS-CoV-2 deISGylation complex that will help guide development of COVID-19 therapeutics targeting this complex. Twit Text FOAVip Conformational Dynamics in the Interaction of SARS-CoV-2 Papain-like Protease with Human Interferon-Stimulated Gene 15 Protein ????J Phys Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=34110168 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34110168 #FOAvip English Wikipedia <ref>{{Cite pmid|34110168}}</ref> Conformational Dynamics in the Interaction of SARS-CoV-2 Papain-like Protease with Human Interferon-Stimulated Gene 15 Protein #MMPMID34110168 Leite WC; Weiss KL; Phillips G; Zhang Q; Qian S; Tsutakawa SE; Coates L; O'Neill H J Phys Chem Lett 2021[Jun]; 12 (23): 5608-5615 PMID34110168show ga Papain-like protease (PLpro) from SARS-CoV-2 plays essential roles in the replication cycle of the virus. In particular, it preferentially interacts with and cleaves human interferon-stimulated gene 15 (hISG15) to suppress the innate immune response of the host. We used small-angle X-ray and neutron scattering combined with computational techniques to study the mechanism of interaction of SARS-CoV-2 PLpro with hISG15. We showed that hISG15 undergoes a transition from an extended to a compact state after binding to PLpro, a conformation that has not been previously observed in complexes of SARS-CoV-2 PLpro with ISG15 from other species. Furthermore, computational analysis showed significant conformational flexibility in the ISG15 N-terminal domain, suggesting that it is weakly bound to PLpro and supports a binding mechanism that is dominated by the C-terminal ISG15 domain. This study fundamentally improves our understanding of the SARS-CoV-2 deISGylation complex that will help guide development of COVID-19 therapeutics targeting this complex. |Coronavirus Papain-Like Proteases/*chemistry/genetics/*metabolism[MESH] |Cytokines/*chemistry/genetics/*metabolism[MESH] |Humans[MESH] |Interferons/*metabolism[MESH] |Neutron Diffraction[MESH] |Protein Conformation[MESH] |SARS-CoV-2/enzymology/genetics/*metabolism[MESH] |Scattering, Small Angle[MESH] |Ubiquitins/*chemistry/genetics/*metabolism[MESH]Conformational Dynamics in the Interaction of SARS-CoV-2 Papain-like P(epmc).pdf DeepDyve Pubget Overpricing