id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-311383-1aqt65cc	Tan, Jinzhi	The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes	2009-05-15		.txt	text/plain	7613	391	58	However, within the large Nsp3 (1922 amino-acid residues), the structure and function of the so-called SARS-unique domain (SUD) have remained elusive. The SARS-CoV genome is devoid of G-stretches longer than 5–6 nucleotides, but more extended G-stretches are found in the 3′-nontranslated regions of mRNAs coding for certain host-cell proteins involved in apoptosis or signal transduction, and have been shown to bind to SUD in vitro. In this communication, we describe the crystal structures at 2.2 Å and 2.8 Å resolution (monoclinic and triclinic form, respectively) of the core of the SARS-unique domain (SUD core , Nsp3 residues 389-652). One potential binding site for G-quadruplexes might be in a cleft between two consecutive SUD core dimers as they occur in both the monoclinic and triclinic crystal forms ( Figure S2B ), but for confirmation, any of these models will have to await crystallographic determination of the complex.	./cache/cord-311383-1aqt65cc.txt	./txt/cord-311383-1aqt65cc.txt