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10.1073/pnas.2008209117 http://scihub22266oqcxt.onion/10.1073/pnas.2008209117 32503918!7322019!32503918     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 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2020 ; 117 (25): 13967-13974 Nephropedia Template TP {{tp|p=32503918|t=2020. Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-bonding and hydrophobic interactions |pdf=|usr=}}{{32503918}} gab.com Text Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-bonding and hydrophobic interactions JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=32503918 #FOAvip Molecular dynamics and free energy simulations have been carried out to elucidate the structural origin of differential protein-protein interactions between the common receptor protein angiotensin converting enzyme 2 (ACE2) and the receptor binding domains of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) [A. E. Gorbalenya et al., Nat. Microbiol. 5, 536-544 (2020)] that causes coronavirus disease 2019 (COVID-19) [P. Zhou et al., Nature 579, 270-273 (2020)] and the SARS coronavirus in the 2002-2003 (SARS-CoV) [T. Kuiken et al., Lancet 362, 263-270 (2003)] outbreak. Analysis of the dynamic trajectories reveals that the binding interface consists of a primarily hydrophobic region and a delicate hydrogen-bonding network in the 2019 novel coronavirus. A key mutation from a hydrophobic residue in the SARS-CoV sequence to Lys417 in SARS-CoV-2 creates a salt bridge across the central hydrophobic contact region, which along with polar residue mutations results in greater electrostatic complementarity than that of the SARS-CoV complex. Furthermore, both electrostatic effects and enhanced hydrophobic packing due to removal of four out of five proline residues in a short 12-residue loop lead to conformation shift toward a more tilted binding groove in the complex in comparison with the SARS-CoV complex. On the other hand, hydrophobic contacts in the complex of the SARS-CoV-neutralizing antibody 80R are disrupted in the SARS-CoV-2 homology complex model, which is attributed to failure of recognition of SARS-CoV-2 by 80R. Twit Text FOAVip Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-bonding and hydrophobic interactions ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=32503918 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32503918 #FOAvip English Wikipedia <ref>{{Cite pmid|32503918}}</ref> Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-bonding and hydrophobic interactions #MMPMID32503918 Wang Y; Liu M; Gao J Proc Natl Acad Sci U S A 2020[Jun]; 117 (25): 13967-13974 PMID32503918show ga Molecular dynamics and free energy simulations have been carried out to elucidate the structural origin of differential protein-protein interactions between the common receptor protein angiotensin converting enzyme 2 (ACE2) and the receptor binding domains of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) [A. E. Gorbalenya et al., Nat. Microbiol. 5, 536-544 (2020)] that causes coronavirus disease 2019 (COVID-19) [P. Zhou et al., Nature 579, 270-273 (2020)] and the SARS coronavirus in the 2002-2003 (SARS-CoV) [T. Kuiken et al., Lancet 362, 263-270 (2003)] outbreak. Analysis of the dynamic trajectories reveals that the binding interface consists of a primarily hydrophobic region and a delicate hydrogen-bonding network in the 2019 novel coronavirus. A key mutation from a hydrophobic residue in the SARS-CoV sequence to Lys417 in SARS-CoV-2 creates a salt bridge across the central hydrophobic contact region, which along with polar residue mutations results in greater electrostatic complementarity than that of the SARS-CoV complex. Furthermore, both electrostatic effects and enhanced hydrophobic packing due to removal of four out of five proline residues in a short 12-residue loop lead to conformation shift toward a more tilted binding groove in the complex in comparison with the SARS-CoV complex. On the other hand, hydrophobic contacts in the complex of the SARS-CoV-neutralizing antibody 80R are disrupted in the SARS-CoV-2 homology complex model, which is attributed to failure of recognition of SARS-CoV-2 by 80R. |*Protein Binding[MESH] |Amino Acids/chemistry[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Antibodies, Neutralizing/metabolism[MESH] |Antibodies, Viral/metabolism[MESH] |Betacoronavirus/*physiology[MESH] |COVID-19[MESH] |Coronavirus Infections[MESH] |Humans[MESH] |Hydrogen Bonding[MESH] |Hydrophobic and Hydrophilic Interactions[MESH] |Models, Molecular[MESH] |Molecular Dynamics Simulation[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/*metabolism[MESH] |Pneumonia, Viral[MESH] |Protein Domains[MESH] |Receptors, Virus/*metabolism[MESH] |SARS-CoV-2[MESH]Enhanced receptor binding of SARS-CoV-2 through networks of hydrogen-b(epmc).pdf DeepDyve Pubget Overpricing