QM/QM studies for Michael reaction in coronavirus main protease (3CLPro)
نویسندگان
چکیده
منابع مشابه
Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro.
SARS (severe acute respiratory syndrome) is caused by a newly discovered coronavirus. A key enzyme for the maturation of this virus and, therefore, a target for drug development is the main protease 3CL(pro) (also termed SARS-CoV 3CL(pro)). We have cloned and expressed in Escherichia coli the full-length SARS-CoV 3CL(pro) as well as a truncated form containing only the catalytic domains. The re...
متن کاملCoronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs.
A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also called 3CLpro), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) Mpro and for an inhibitor complex of porcine coronavirus [t...
متن کاملStructure of Main Protease from Human Coronavirus NL63: Insights for Wide Spectrum Anti-Coronavirus Drug Design
First identified in The Netherlands in 2004, human coronavirus NL63 (HCoV-NL63) was found to cause worldwide infections. Patients infected by HCoV-NL63 are typically young children with upper and lower respiratory tract infection, presenting with symptoms including croup, bronchiolitis, and pneumonia. Unfortunately, there are currently no effective antiviral therapy to contain HCoV-NL63 infecti...
متن کاملTemperature-sensitive mutants and revertants in the coronavirus nonstructural protein 5 protease (3CLpro) define residues involved in long-distance communication and regulation of protease activity.
Positive-strand RNA virus genomes are translated into polyproteins that are processed by viral proteases to yield functional intermediate and mature proteins. Coronaviruses (CoVs) carry genes that encode an nsp5 protease (also known as 3CLpro or Mpro) responsible for 11 maturation cleavages. The nsp5 structure contains two chymotrypsin-like domains (D1 and D2) and a unique domain (D3), and form...
متن کاملSubstrate specificity and rational design of peptidomimetic inhibitors for SARS coronavirus main protease.
The main protease (Mpro) of severe acute respiratory syndrome coronavirus (SARS CoV) is a key enzyme for viral replication, and is thus an attractive target for anti-SARS CoV drug development. Mpro belongs to the family of 3C-like cysteine proteases. The basic design of peptidomimetic inhibitors involved a warhead that can form covalent modifications to the –SH group of the active site residue ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Molecular Graphics and Modelling
سال: 2008
ISSN: 1093-3263
DOI: 10.1016/j.jmgm.2008.05.002