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10.1073/pnas.2021785118 http://scihub22266oqcxt.onion/10.1073/pnas.2021785118 33361333!7812859!33361333     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33361333&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (2): ? Nephropedia Template TP {{tp|p=33361333|t=2021. Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein |pdf=|usr=}}{{33361333}} gab.com Text Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33361333 #FOAvip The molecular basis for the severity and rapid spread of the COVID-19 disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely unknown. ORF8 is a rapidly evolving accessory protein that has been proposed to interfere with immune responses. The crystal structure of SARS-CoV-2 ORF8 was determined at 2.04-A resolution by X-ray crystallography. The structure reveals a approximately 60-residue core similar to SARS-CoV-2 ORF7a, with the addition of two dimerization interfaces unique to SARS-CoV-2 ORF8. A covalent disulfide-linked dimer is formed through an N-terminal sequence specific to SARS-CoV-2, while a separate noncovalent interface is formed by another SARS-CoV-2-specific sequence, (73)YIDI(76) Together, the presence of these interfaces shows how SARS-CoV-2 ORF8 can form unique large-scale assemblies not possible for SARS-CoV, potentially mediating unique immune suppression and evasion activities. Twit Text FOAVip Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33361333 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33361333 #FOAvip English Wikipedia <ref>{{Cite pmid|33361333}}</ref> Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein #MMPMID33361333 Flower TG; Buffalo CZ; Hooy RM; Allaire M; Ren X; Hurley JH Proc Natl Acad Sci U S A 2021[Jan]; 118 (2): ? PMID33361333show ga The molecular basis for the severity and rapid spread of the COVID-19 disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely unknown. ORF8 is a rapidly evolving accessory protein that has been proposed to interfere with immune responses. The crystal structure of SARS-CoV-2 ORF8 was determined at 2.04-A resolution by X-ray crystallography. The structure reveals a approximately 60-residue core similar to SARS-CoV-2 ORF7a, with the addition of two dimerization interfaces unique to SARS-CoV-2 ORF8. A covalent disulfide-linked dimer is formed through an N-terminal sequence specific to SARS-CoV-2, while a separate noncovalent interface is formed by another SARS-CoV-2-specific sequence, (73)YIDI(76) Together, the presence of these interfaces shows how SARS-CoV-2 ORF8 can form unique large-scale assemblies not possible for SARS-CoV, potentially mediating unique immune suppression and evasion activities. |*Molecular Structure[MESH] |Evolution, Molecular[MESH] |Immune Evasion[MESH] |SARS-CoV-2/*chemistry[MESH]Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protei(epmc).pdf DeepDyve Pubget Overpricing