Structural Changes at the Zinc Active Site of ACE2 on Binding the SARS-CoV-2 Spike Protein Receptor Binding Domain

Inorganic Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 17, 2025

The causative agent of Covid-19 is the SARS-CoV-2 virus. Initiation cell entry by critically dependent upon binding spike protein to angiotensin-converting enzyme 2 (ACE2, EC 3.4.17.23). mechanism receptor domain ACE2 among most intensively studied infection mechanisms any pathogen, including a very large number structural studies. membrane-associated zinc carboxypeptidase, comprising three domains, protease domain, neck and membrane-spanning α-helical domain. In addition its role as also chaperone for Na+–amino acid cotransporter called B0AT1, in presence full-length forms dimers. Most studies date related have employed just neglected possible roles Zn2+-containing active site. We show here that ACE2, (and absence B0AT1), dimeric shows distinctive allostery catalytic activity. contrast, monomeric no allostery. Binding (RBD) eliminates X-ray absorption spectroscopy Zn2+ changes site structure RBD but only form. Taken together, our results indicate exhibits notable level flexibility form both likely presents superior model study ACE2-spike interactions than ACE2.

Language: Английский

VII Congress of Russian Biophysicists—2023, Krasnodar, Russia

Biophysical Reviews, Journal Year: 2023, Volume and Issue: unknown

Published: Oct. 13, 2023

Language: Английский