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10.1107/S2052252520009653 http://scihub22266oqcxt.onion/10.1107/S2052252520009653 32939273!7467174!32939273     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       IUCrJ 2020 ; 7 (Pt 5): 814-824 Nephropedia Template TP {{tp|p=32939273|t=2020. Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes |pdf=|usr=}}{{32939273}} gab.com Text Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes JO: IUCrJ http://www.kidney.de/pget.php?&tw=1&pmid=32939273 #FOAvip Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07-2.01 A) crystal structures corresponding to the apo form of the protein and its complexes with 2-(N-morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics. Twit Text FOAVip Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes ????IUCrJ http://www.kidney.de/pget.php?&tw=1&pmid=32939273 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32939273 #FOAvip English Wikipedia <ref>{{Cite pmid|32939273}}</ref> Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes #MMPMID32939273 Michalska K; Kim Y; Jedrzejczak R; Maltseva NI; Stols L; Endres M; Joachimiak A IUCrJ 2020[Sep]; 7 (Pt 5): 814-824 PMID32939273show ga Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07-2.01 A) crystal structures corresponding to the apo form of the protein and its complexes with 2-(N-morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics. äCrystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo (epmc).pdf DeepDyve Pubget Overpricing