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10.1126/science.abd3255 http://scihub22266oqcxt.onion/10.1126/science.abd3255 32958580!8050947!32958580     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32958580&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 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\32958580.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Science 2020 ; 370 (6517): 725-730 Nephropedia Template TP {{tp|p=32958580|t=2020. Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein |pdf=|usr=}}{{32958580}} gab.com Text Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32958580 #FOAvip Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), represents a global crisis. Key to SARS-CoV-2 therapeutic development is unraveling the mechanisms that drive high infectivity, broad tissue tropism, and severe pathology. Our 2.85-angstrom cryo-electron microscopy structure of SARS-CoV-2 spike (S) glycoprotein reveals that the receptor binding domains tightly bind the essential free fatty acid linoleic acid (LA) in three composite binding pockets. A similar pocket also appears to be present in the highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV). LA binding stabilizes a locked S conformation, resulting in reduced angiotensin-converting enzyme 2 (ACE2) interaction in vitro. In human cells, LA supplementation synergizes with the COVID-19 drug remdesivir, suppressing SARS-CoV-2 replication. Our structure directly links LA and S, setting the stage for intervention strategies that target LA binding by SARS-CoV-2. Twit Text FOAVip Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32958580 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32958580 #FOAvip English Wikipedia <ref>{{Cite pmid|32958580}}</ref> Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein #MMPMID32958580 Toelzer C; Gupta K; Yadav SKN; Borucu U; Davidson AD; Kavanagh Williamson M; Shoemark DK; Garzoni F; Staufer O; Milligan R; Capin J; Mulholland AJ; Spatz J; Fitzgerald D; Berger I; Schaffitzel C Science 2020[Nov]; 370 (6517): 725-730 PMID32958580show ga Coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), represents a global crisis. Key to SARS-CoV-2 therapeutic development is unraveling the mechanisms that drive high infectivity, broad tissue tropism, and severe pathology. Our 2.85-angstrom cryo-electron microscopy structure of SARS-CoV-2 spike (S) glycoprotein reveals that the receptor binding domains tightly bind the essential free fatty acid linoleic acid (LA) in three composite binding pockets. A similar pocket also appears to be present in the highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV). LA binding stabilizes a locked S conformation, resulting in reduced angiotensin-converting enzyme 2 (ACE2) interaction in vitro. In human cells, LA supplementation synergizes with the COVID-19 drug remdesivir, suppressing SARS-CoV-2 replication. Our structure directly links LA and S, setting the stage for intervention strategies that target LA binding by SARS-CoV-2. |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Betacoronavirus[MESH] |Binding Sites[MESH] |Chlorocebus aethiops[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Linoleic Acid/*metabolism[MESH] |Middle East Respiratory Syndrome Coronavirus[MESH] |Models, Molecular[MESH] |Peptidyl-Dipeptidase A/metabolism[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Structure, Tertiary[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/ultrastructure[MESH]Free fatty acid binding pocket in the locked structure of SARS-CoV-2 s(epmc).pdf DeepDyve Pubget Overpricing