tetano
Editor, Senior Moderator
Science. 2020 Mar 4. pii: eabb2762. doi: 10.1126/science.abb2762. [Epub ahead of print] [h=1]Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2.[/h]
Yan R[SUP]1,[/SUP][SUP]2[/SUP], Zhang Y[SUP]1,[/SUP][SUP]2[/SUP], Li Y[SUP]3[/SUP], Xia L[SUP]1,[/SUP][SUP]2[/SUP], Guo Y[SUP]1,[/SUP][SUP]2[/SUP], Zhou Q[SUP]4,[/SUP][SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for SARS coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious epidemic COVID-19. Here we present cryo-EM structures of full-length human ACE2, in the presence of a neutral amino acid transporter B[SUP]0[/SUP]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 ?, with a local resolution of 3.5 ? at the ACE2-RBD interface. The ACE2-B[SUP]0[/SUP]AT1 complex is assembled as a dimer of heterodimers, with the Collectrin-like domain (CLD) of ACE2 mediating homo-dimerization. The RBD is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. These findings provide important insights to the molecular basis for coronavirus recognition and infection.
Copyright ? 2020, American Association for the Advancement of Science.
PMID: 32132184 DOI: 10.1126/science.abb2762
Yan R[SUP]1,[/SUP][SUP]2[/SUP], Zhang Y[SUP]1,[/SUP][SUP]2[/SUP], Li Y[SUP]3[/SUP], Xia L[SUP]1,[/SUP][SUP]2[/SUP], Guo Y[SUP]1,[/SUP][SUP]2[/SUP], Zhou Q[SUP]4,[/SUP][SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for SARS coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious epidemic COVID-19. Here we present cryo-EM structures of full-length human ACE2, in the presence of a neutral amino acid transporter B[SUP]0[/SUP]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 ?, with a local resolution of 3.5 ? at the ACE2-RBD interface. The ACE2-B[SUP]0[/SUP]AT1 complex is assembled as a dimer of heterodimers, with the Collectrin-like domain (CLD) of ACE2 mediating homo-dimerization. The RBD is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. These findings provide important insights to the molecular basis for coronavirus recognition and infection.
Copyright ? 2020, American Association for the Advancement of Science.
PMID: 32132184 DOI: 10.1126/science.abb2762