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10.3389/fmolb.2021.666626 http://scihub22266oqcxt.onion/10.3389/fmolb.2021.666626 33996911!8119889!33996911     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       Front+Mol+Biosci 2021 ; 8 (ä): 666626 Nephropedia Template TP {{tp|p=33996911|t=2021. Computational Identification of a Putative Allosteric Binding Pocket in TMPRSS2 |pdf=|usr=}}{{33996911}} gab.com Text Computational Identification of a Putative Allosteric Binding Pocket in TMPRSS2 JO: Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=33996911 #FOAvip Camostat, nafamostat, and bromhexine are inhibitors of the transmembrane serine protease TMPRSS2. The inhibition of TMPRSS2 has been shown to prevent the viral infection of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and other viruses. However, while camostat and nafamostat inhibit TMPRSS2 by forming a covalent adduct, the mode of action of bromhexine remains unclear. TMPRSS2 is autocatalytically activated from its inactive form, zymogen, through a proteolytic cleavage that promotes the binding of Ile256 to a putative allosteric pocket (A-pocket). Computer simulations, reported here, indicate that Ile256 binding induces a conformational change in the catalytic site, thus providing the atomistic rationale to the activation process of the enzyme. Furthermore, computational docking and molecular dynamics simulations indicate that bromhexine competes with the N-terminal Ile256 for the same binding site, making it a potential allosteric inhibitor. Taken together, these findings provide the atomistic basis for the development of more selective and potent TMPRSS2 inhibitors. Twit Text FOAVip Computational Identification of a Putative Allosteric Binding Pocket in TMPRSS2 ????Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=33996911 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33996911 #FOAvip English Wikipedia <ref>{{Cite pmid|33996911}}</ref> Computational Identification of a Putative Allosteric Binding Pocket in TMPRSS2 #MMPMID33996911 Sgrignani J; Cavalli A Front Mol Biosci 2021[]; 8 (ä): 666626 PMID33996911show ga Camostat, nafamostat, and bromhexine are inhibitors of the transmembrane serine protease TMPRSS2. The inhibition of TMPRSS2 has been shown to prevent the viral infection of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and other viruses. However, while camostat and nafamostat inhibit TMPRSS2 by forming a covalent adduct, the mode of action of bromhexine remains unclear. TMPRSS2 is autocatalytically activated from its inactive form, zymogen, through a proteolytic cleavage that promotes the binding of Ile256 to a putative allosteric pocket (A-pocket). Computer simulations, reported here, indicate that Ile256 binding induces a conformational change in the catalytic site, thus providing the atomistic rationale to the activation process of the enzyme. Furthermore, computational docking and molecular dynamics simulations indicate that bromhexine competes with the N-terminal Ile256 for the same binding site, making it a potential allosteric inhibitor. Taken together, these findings provide the atomistic basis for the development of more selective and potent TMPRSS2 inhibitors. äComputational Identification of a Putative Allosteric Binding Pocket i(epmc).pdf DeepDyve Pubget Overpricing