Mutation of Asn28 disrupts the dimerization and enzymatic activity of SARS 3CL(pro) .

ABSTRACT: Coronaviruses are responsible for a significant proportion of annual respiratory and enteric infections in humans and other mammals. The most prominent of these viruses is the severe acute respiratory syndrome coronavirus (SARS-CoV) which causes acute respiratory and gastrointestinal infection in humans. The coronavirus main protease, 3CL(pro), is a key target for broad-spectrum antiviral development because of its critical role in viral maturation and high degree of structural conservation among coronaviruses. Dimerization is an indispensable requirement for the function of SARS 3CL(pro) and is regulated through mechanisms involving both direct and long-range interactions in the enzyme. While many of the binding interactions at the dimerization interface have been extensively studied, tho

SUBMITTER: Barrila J 

PROVIDER: S-EPMC2877132 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature