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10.1002/pro.15

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suck abstract from ncbi


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pmid19177346      Protein+Sci 2009 ; 18 (1): 6-16
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  • Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property #MMPMID19177346
  • Piotrowski Y; Hansen G; Boomaars-van der Zanden AL; Snijder EJ; Gorbalenya AE; Hilgenfeld R
  • Protein Sci 2009[Jan]; 18 (1): 6-16 PMID19177346show ga
  • The polyproteins of coronaviruses are cleaved by viral proteases into at least 15 nonstructural proteins (Nsps). Consisting of five domains, Nsp3 is the largest of these (180-210 kDa). Among these domains, the so-called X-domain is believed to act as ADP-ribose-1''-phosphate phosphatase or to bind poly(ADP-ribose). However, here we show that the X-domain of Infectious Bronchitis Virus (strain Beaudette), a Group-3 coronavirus, fails to bind ADP-ribose. This is explained on the basis of the crystal structure of the protein, determined at two different pH values. For comparison, we also describe the crystal structure of the homologous X-domain from Human Coronavirus 229E, a Group-1 coronavirus, which does bind ADP-ribose.
  • |Adenosine Diphosphate Ribose/analogs & derivatives/chemistry/*metabolism[MESH]
  • |Amino Acid Sequence[MESH]
  • |Coronavirus 229E, Human/*chemistry/genetics/metabolism[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Infectious bronchitis virus/*chemistry/genetics/metabolism[MESH]
  • |Models, Molecular[MESH]
  • |Molecular Sequence Data[MESH]
  • |Phosphoric Monoester Hydrolases/chemistry/genetics/metabolism[MESH]
  • |Protein Binding/physiology[MESH]
  • |Protein Conformation[MESH]
  • |Sequence Alignment[MESH]
  • |Severe acute respiratory syndrome-related coronavirus/chemistry/genetics/metabolism[MESH]


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