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

• Tác giả: Julien J H Cotelesage, Miroslaw Cygler, Natalia V Dolgova, Graham N George, Andrey Grishin, Thomas Kroll, Matthew Latimer, Ingrid J Pickering, Muhammad Qureshi, Dimosthenis Sokaras, Linda I Vogt
• Ngôn ngữ: eng
• Ký hiệu phân loại: 781.726 *Holy Week
• Thông tin xuất bản: United States : Inorganic chemistry , 2025
• Bộ sưu tập: NCBI
• ID: 185059

Tóm tắt

The causative agent of Covid-19 is the SARS-CoV-2 virus. Initiation of cell entry by SARS-CoV-2 is critically dependent upon binding of the SARS-CoV-2 spike protein to angiotensin-converting enzyme 2 (ACE2, EC 3.4.17.23). The mechanism of binding of the SARS-CoV-2 spike receptor binding domain to ACE2 is among the most intensively studied infection mechanisms of any pathogen, including a very large number of structural studies. ACE2 is a membrane-associated zinc carboxypeptidase, comprising three domains, the protease domain, a neck domain, and a membrane-spanning α-helical domain. In addition to its role as a carboxypeptidase, ACE2 is also a chaperone for a Na