About: The newly emerging human pathogen, Middle East respiratory syndrome coronavirus (MERS-CoV), contains a macro domain in the highly conserved N-terminal region of non-structural protein 3. Intense research has shown that macro domains bind ADP-ribose and other derivatives, but it still remains intangible about their exact function. In this study we report the preliminary structural analysis through solution NMR spectroscopy of the MERS-CoV macro domain. The near complete NMR assignments of MERS-CoV macro domain provide the basis for subsequent structural and biochemical investigation in the context of protein function.   Goto Sponge  NotDistinct  Permalink

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  • The newly emerging human pathogen, Middle East respiratory syndrome coronavirus (MERS-CoV), contains a macro domain in the highly conserved N-terminal region of non-structural protein 3. Intense research has shown that macro domains bind ADP-ribose and other derivatives, but it still remains intangible about their exact function. In this study we report the preliminary structural analysis through solution NMR spectroscopy of the MERS-CoV macro domain. The near complete NMR assignments of MERS-CoV macro domain provide the basis for subsequent structural and biochemical investigation in the context of protein function.
Subject
  • Middle East respiratory syndrome
  • Zoonoses
  • Viral respiratory tract infections
  • Spectroscopy
  • 2012 in Saudi Arabia
  • 2013 in Saudi Arabia
  • Animal viral diseases
  • Death in Saudi Arabia
  • Health in Saudi Arabia
  • Bat virome
  • Chiroptera-borne diseases
  • Merbecovirus
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