Selected article for: "SUD core and zone interference"
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_46
    Snippet: Protein Data Bank: Coordinates and structure factors have been deposited with accession code 2W2G (P2 1 crystal form) and 2WCT (P1 crystal form). Figure S1 Zone-interference gel electrophoresis experiment showing that SUD core fails to bind NAD+ and ADP-ribose. SUD core alone (label 0) and decreasing concentrations (1, 0.5, 0.1, 0.05 and 0.02 mM) of NAD + , or decreasing concentrations (1, 0.5, 0.1, 0.05 and 0.02 mM) of ADP-ribose. Found at: doi:.....
    Document: Protein Data Bank: Coordinates and structure factors have been deposited with accession code 2W2G (P2 1 crystal form) and 2WCT (P1 crystal form). Figure S1 Zone-interference gel electrophoresis experiment showing that SUD core fails to bind NAD+ and ADP-ribose. SUD core alone (label 0) and decreasing concentrations (1, 0.5, 0.1, 0.05 and 0.02 mM) of NAD + , or decreasing concentrations (1, 0.5, 0.1, 0.05 and 0.02 mM) of ADP-ribose. Found at: doi:10.1371/journal.ppat.1000428.s001 (0.70 MB DOC) Figure S2 Alternative models of G-quadruplex binding to SUD core , obtained by automated docking into the crystal structures. The SUD-N and SUD-M subdomains are in violet and cyan, respectively, the G-quadruplex as found in the bcl-2 promoter region (PDB code: 2F8U) is in orange. The pairs of mutations in SUD-N are indicated by green (M1, K505A+K506A) and blue (M2, K476A+K477A) spheres. The M3 set of mutations in SUD-M is indicated by olive (K563A) and orange (K565A+K568A) spheres. The M4 set of mutations, also in SUD-M, is indicated by orange (K565A+K568A) and yellow (E571A) spheres. (A) A possible binding site is in a cleft between monomers in the SUD core dimer. The binding site is close to the lysine residues replaced by the M3 and M4 mutations, compatible with the inability of these mutants to bind G-quadruplexes. (B) A second potential binding site is a cleft between two neighboring SUD core dimers as found in both crystal packing arrangements (space groups P2 1 and P1). This binding mode is compatible with the observation of SUD core oligomerization upon G-quadruplex binding.

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