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10.1002/prot.26143 http://scihub22266oqcxt.onion/10.1002/prot.26143 33983654!8242809!33983654     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33983654&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 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proteins 2021 ; 89 (9): 1216-1225 Nephropedia Template TP {{tp|p=33983654|t=2021. Comparative protein structure network analysis on 3CL(pro) from SARS-CoV-1 and SARS-CoV-2 |pdf=|usr=}}{{33983654}} gab.com Text Comparative protein structure network analysis on 3CL(pro) from SARS-CoV-1 and SARS-CoV-2 JO: Proteins http://www.kidney.de/pget.php?&tw=1&pmid=33983654 #FOAvip The main protease M(pro) , 3CL(pro) is an important target from coronaviruses. In spite of having 96% sequence identity among M(pros) from SARS-CoV-1 and SARS-CoV-2; the inhibitors used to block the activity of SARS-CoV-1 M(pro) so far, were found to have differential inhibitory effect on M(pro) of SARS-CoV-2. The possible reason could be due to the difference of few amino acids among the peptidases. Since, overall 3-D crystallographic structure of M(pro) from SARS-CoV-1 and SARS-CoV-2 is quite similar and mapping a subtle structural variation is seemingly impossible. Hence, we have attempted to study a structural comparison of SARS-CoV-1 and SARS-CoV-2 M(pro) in apo and inhibitor bound states using protein structure network (PSN) based approach at contacts level. The comparative PSNs analysis of apo M(pros) from SARS-CoV-1 and SARS-CoV-2 uncovers small but significant local changes occurring near the active site region and distributed throughout the structure. Additionally, we have shown how inhibitor binding perturbs the PSG and the communication pathways in M(pros) . Moreover, we have also investigated the network connectivity on the quaternary structure of M(pro) and identified critical residue pairs for complex formation using three centrality measurement parameters along with the modularity analysis. Taken together, these results on the comparative PSN provide an insight into conformational changes that may be used as an additional guidance towards specific drug development. Twit Text FOAVip Comparative protein structure network analysis on 3CL(pro) from SARS-CoV-1 and SARS-CoV-2 ????Proteins http://www.kidney.de/pget.php?&tw=1&pmid=33983654 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33983654 #FOAvip English Wikipedia <ref>{{Cite pmid|33983654}}</ref> Comparative protein structure network analysis on 3CL(pro) from SARS-CoV-1 and SARS-CoV-2 #MMPMID33983654 Lata S; Akif M Proteins 2021[Sep]; 89 (9): 1216-1225 PMID33983654show ga The main protease M(pro) , 3CL(pro) is an important target from coronaviruses. In spite of having 96% sequence identity among M(pros) from SARS-CoV-1 and SARS-CoV-2; the inhibitors used to block the activity of SARS-CoV-1 M(pro) so far, were found to have differential inhibitory effect on M(pro) of SARS-CoV-2. The possible reason could be due to the difference of few amino acids among the peptidases. Since, overall 3-D crystallographic structure of M(pro) from SARS-CoV-1 and SARS-CoV-2 is quite similar and mapping a subtle structural variation is seemingly impossible. Hence, we have attempted to study a structural comparison of SARS-CoV-1 and SARS-CoV-2 M(pro) in apo and inhibitor bound states using protein structure network (PSN) based approach at contacts level. The comparative PSNs analysis of apo M(pros) from SARS-CoV-1 and SARS-CoV-2 uncovers small but significant local changes occurring near the active site region and distributed throughout the structure. Additionally, we have shown how inhibitor binding perturbs the PSG and the communication pathways in M(pros) . Moreover, we have also investigated the network connectivity on the quaternary structure of M(pro) and identified critical residue pairs for complex formation using three centrality measurement parameters along with the modularity analysis. Taken together, these results on the comparative PSN provide an insight into conformational changes that may be used as an additional guidance towards specific drug development. |Apoenzymes/antagonists & inhibitors/chemistry/metabolism[MESH] |Binding Sites[MESH] |Coronavirus 3C Proteases/antagonists & inhibitors/*chemistry/metabolism[MESH] |Holoenzymes/chemistry/metabolism[MESH] |Models, Molecular[MESH] |Protease Inhibitors/pharmacology[MESH] |Protein Multimerization/drug effects[MESH] |Protein Structure, Quaternary/drug effects[MESH] |SARS-CoV-2/*enzymology[MESH]Comparative protein structure network analysis on 3CL(pro) from SARS-C(epmc).pdf DeepDyve Pubget Overpricing