Author: Tan, Jinzhi; Vonrhein, Clemens; Smart, Oliver S.; Bricogne, Gerard; Bollati, Michela; Kusov, Yuri; Hansen, Guido; Mesters, Jeroen R.; Schmidt, Christian L.; Hilgenfeld, Rolf
Title: The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes Document date: 2009_5_15
ID: 1aqt65cc_1
Snippet: The SARS coronavirus (SARS-CoV) is much more pathogenic for humans than any other coronavirus. Therefore, protein domains encoded by the SARS-CoV genome that are absent in other coronaviruses are of particular interest, because they may be responsible for the extraordinary virulence. The most prominent such domain has been identified by bioinformatics as part of nonstructural protein 3 (Nsp3) of the virus and appropriately named the ''SARS-unique.....
Document: The SARS coronavirus (SARS-CoV) is much more pathogenic for humans than any other coronavirus. Therefore, protein domains encoded by the SARS-CoV genome that are absent in other coronaviruses are of particular interest, because they may be responsible for the extraordinary virulence. The most prominent such domain has been identified by bioinformatics as part of nonstructural protein 3 (Nsp3) of the virus and appropriately named the ''SARS-unique domain'' (SUD) [1] . With a molecular mass of 213 kDa, Nsp3 is the largest of the non-structural proteins of SARS coronavirus (see Figure 1 ). Comprising 1922 amino-acid residues (polyprotein 1a/1ab residues Ala819 to Gly2740), SARS-CoV Nsp3 is larger than the entire replicase of Picornaviridae. It contains at least seven subdomains [2] : An N-terminal acidic domain (Ac, also called Nsp3a); an X-domain (also designated as ADRP, or Nsp3b); the SUD (Nsp3c); a papain-like proteinase, PL2 pro (also called Nsp3d); and additional domains (Nsp3e-g) that include a transmembrane (TM) region.
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