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10.1126/science.abb2762 http://scihub22266oqcxt.onion/10.1126/science.abb2762 32132184!7164635!32132184     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 367 (6485): 1444-1448 Nephropedia Template TP {{tp|p=32132184|t=2020. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 |pdf=|usr=}}{{32132184}} gab.com Text Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32132184 #FOAvip Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B(0)AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B(0)AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection. Twit Text FOAVip Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32132184 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32132184 #FOAvip English Wikipedia <ref>{{Cite pmid|32132184}}</ref> Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 #MMPMID32132184 Yan R; Zhang Y; Li Y; Xia L; Guo Y; Zhou Q Science 2020[Mar]; 367 (6485): 1444-1448 PMID32132184show ga Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B(0)AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B(0)AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection. |Amino Acid Sequence[MESH] |Amino Acid Transport Systems, Neutral/*ultrastructure[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Betacoronavirus[MESH] |COVID-19[MESH] |Coronavirus Infections[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/*ultrastructure[MESH] |Pneumonia, Viral[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |Receptors, Virus/*ultrastructure[MESH] |SARS-CoV-2[MESH] |Sequence Alignment[MESH] |Severe acute respiratory syndrome-related coronavirus[MESH]Structural basis for the recognition of SARS-CoV-2 by full-length huma(epmc).pdf DeepDyve Pubget Overpricing