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10.1002/prot.26024 http://scihub22266oqcxt.onion/10.1002/prot.26024 33210300!7753379!33210300     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proteins 2021 ; 89 (4): 389-398 Nephropedia Template TP {{tp|p=33210300|t=2021. Why are ACE2 binding coronavirus strains SARS-CoV/SARS-CoV-2 wild and NL63 mild?|pdf=|usr=}}{{33210300}} gab.com Text Why are ACE2 binding coronavirus strains SARS-CoV/SARS-CoV-2 wild and NL63 mild JO: Proteins http://www.kidney.de/pget.php?&tw=1&pmid=33210300 #FOAvip Coronaviruses are responsible for several epidemics, including the 2002 SARS, 2012 MERS, and COVID-19. The emergence of recent COVID-19 pandemic due to SARS-CoV-2 virus in December 2019 has resulted in considerable research efforts to design antiviral drugs and other therapeutics against coronaviruses. In this context, it is crucial to understand the biophysical and structural features of the major proteins that are involved in virus-host interactions. In the current study, we have compared spike proteins from three strains of coronaviruses NL63, SARS-CoV, and SARS-CoV, known to bind human angiotensin-converting enzyme 2 (ACE2), in terms of sequence/structure conservation, hydrophobic cluster formation and importance of binding site residues. The study reveals that the severity of coronavirus strains correlates positively with the interaction area, surrounding hydrophobicity and interaction energy and inversely correlate with the flexibility of the binding interface. Also, we identify the conserved residues in the binding interface of spike proteins in all three strains. The systematic point mutations show that these conserved residues in the respective strains are evolutionarily favored at their respective positions. The similarities and differences in the spike proteins of the three viruses indicated in this study may help researchers to deeply understand the structural behavior, binding site properties and etiology of ACE2 binding, accelerating the screening of potential lead molecules and the development/repurposing of therapeutic drugs. Twit Text FOAVip Why are ACE2 binding coronavirus strains SARS-CoV/SARS-CoV-2 wild and NL63 mild ????Proteins http://www.kidney.de/pget.php?&tw=1&pmid=33210300 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33210300 #FOAvip English Wikipedia <ref>{{Cite pmid|33210300}}</ref> Why are ACE2 binding coronavirus strains SARS-CoV/SARS-CoV-2 wild and NL63 mild? #MMPMID33210300 Rawat P; Jemimah S; Ponnuswamy PK; Gromiha MM Proteins 2021[Apr]; 89 (4): 389-398 PMID33210300show ga Coronaviruses are responsible for several epidemics, including the 2002 SARS, 2012 MERS, and COVID-19. The emergence of recent COVID-19 pandemic due to SARS-CoV-2 virus in December 2019 has resulted in considerable research efforts to design antiviral drugs and other therapeutics against coronaviruses. In this context, it is crucial to understand the biophysical and structural features of the major proteins that are involved in virus-host interactions. In the current study, we have compared spike proteins from three strains of coronaviruses NL63, SARS-CoV, and SARS-CoV, known to bind human angiotensin-converting enzyme 2 (ACE2), in terms of sequence/structure conservation, hydrophobic cluster formation and importance of binding site residues. The study reveals that the severity of coronavirus strains correlates positively with the interaction area, surrounding hydrophobicity and interaction energy and inversely correlate with the flexibility of the binding interface. Also, we identify the conserved residues in the binding interface of spike proteins in all three strains. The systematic point mutations show that these conserved residues in the respective strains are evolutionarily favored at their respective positions. The similarities and differences in the spike proteins of the three viruses indicated in this study may help researchers to deeply understand the structural behavior, binding site properties and etiology of ACE2 binding, accelerating the screening of potential lead molecules and the development/repurposing of therapeutic drugs. |*Coronavirus NL63, Human[MESH] |*SARS-CoV-2[MESH] |*Severe acute respiratory syndrome-related coronavirus[MESH] |Angiotensin-Converting Enzyme 2/*metabolism[MESH] |Antiviral Agents/pharmacology[MESH] |COVID-19/*virology[MESH] |Coronavirus Infections/virology[MESH] |DNA Mutational Analysis[MESH] |Humans[MESH] |Hydrophobic and Hydrophilic Interactions[MESH] |Ligands[MESH] |Models, Statistical[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Species Specificity[MESH]Why are ACE2 binding coronavirus strains SARS-CoV/SARS-CoV-2 wild and (epmc).pdf DeepDyve Pubget Overpricing