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10.1016/j.jmb.2021.167118 http://scihub22266oqcxt.onion/10.1016/j.jmb.2021.167118 34174328!8223035!34174328     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2021 ; 433 (18): 167118 Nephropedia Template TP {{tp|p=34174328|t=2021. A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Process |pdf=|usr=}}{{34174328}} gab.com Text A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Process JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=34174328 #FOAvip SARS-CoV-2 is the causative agent of COVID-19. The dimeric form of the viral M(pro) is responsible for the cleavage of the viral polyprotein in 11 sites, including its own N and C-terminus. The lack of structural information for intermediary forms of M(pro) is a setback for the understanding its self-maturation process. Herein, we used X-ray crystallography combined with biochemical data to characterize multiple forms of SARS-CoV-2 M(pro). For the immature form, we show that extra N-terminal residues caused conformational changes in the positioning of domain-three over the active site, hampering the dimerization and diminishing its activity. We propose that this form preludes the cis and trans-cleavage of N-terminal residues. Using fragment screening, we probe new cavities in this form which can be used to guide therapeutic development. Furthermore, we characterized a serine site-directed mutant of the M(pro) bound to its endogenous N and C-terminal residues during dimeric association stage of the maturation process. We suggest this form is a transitional state during the C-terminal trans-cleavage. This data sheds light in the structural modifications of the SARS-CoV-2 main protease during its self-maturation process. Twit Text FOAVip A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Process ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=34174328 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34174328 #FOAvip English Wikipedia <ref>{{Cite pmid|34174328}}</ref> A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Process #MMPMID34174328 Noske GD; Nakamura AM; Gawriljuk VO; Fernandes RS; Lima GMA; Rosa HVD; Pereira HD; Zeri ACM; Nascimento AFZ; Freire MCLC; Fearon D; Douangamath A; von Delft F; Oliva G; Godoy AS J Mol Biol 2021[Sep]; 433 (18): 167118 PMID34174328show ga SARS-CoV-2 is the causative agent of COVID-19. The dimeric form of the viral M(pro) is responsible for the cleavage of the viral polyprotein in 11 sites, including its own N and C-terminus. The lack of structural information for intermediary forms of M(pro) is a setback for the understanding its self-maturation process. Herein, we used X-ray crystallography combined with biochemical data to characterize multiple forms of SARS-CoV-2 M(pro). For the immature form, we show that extra N-terminal residues caused conformational changes in the positioning of domain-three over the active site, hampering the dimerization and diminishing its activity. We propose that this form preludes the cis and trans-cleavage of N-terminal residues. Using fragment screening, we probe new cavities in this form which can be used to guide therapeutic development. Furthermore, we characterized a serine site-directed mutant of the M(pro) bound to its endogenous N and C-terminal residues during dimeric association stage of the maturation process. We suggest this form is a transitional state during the C-terminal trans-cleavage. This data sheds light in the structural modifications of the SARS-CoV-2 main protease during its self-maturation process. |Catalytic Domain/physiology[MESH] |Crystallography, X-Ray/methods[MESH] |Dimerization[MESH] |Humans[MESH] |Peptide Hydrolases/*chemistry/*metabolism[MESH] |SARS-CoV-2/*metabolism[MESH]A Crystallographic Snapshot of SARS-CoV-2 Main Protease Maturation Pro(epmc).pdf DeepDyve Pubget Overpricing