The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 Å resolution

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Autor/in:
Erscheinungsjahr:
2010
Medientyp:
Text
Schlagworte:
  • Uridine
  • Fluorouracil
  • Uridine Phosphorylase
  • Adenosine
  • Purinergic P2X7 Receptors
  • Adenosine Triphosphate
  • Uridine
  • Fluorouracil
  • Uridine Phosphorylase
  • Adenosine
  • Purinergic P2X7 Receptors
  • Adenosine Triphosphate
Beschreibung:
  • Uridine nucleoside phosphorylase is an important drug target for the development of anti-infective and antitumour agents. The X-ray crystal structure of Salmonella typhimurium uridine nucleoside phosphorylase (StUPh) complexed with its inhibitor 2,2'-anhydrouridine, phosphate and potassium ions has been solved and refined at 1.86 angstrom resolution (R-cryst = 17.6\%, R-free = 20.6\%). The complex of human uridine phosphorylase I (HUPhI) with 2,2'-anhydrouridine was modelled using a computational approach. The model allowed the identification of atomic groups in 2,2'-anhydrouridine that might improve the interaction of future inhibitors with StUPh and HUPhI.
Lizenz:
  • info:eu-repo/semantics/restrictedAccess
Quellsystem:
Forschungsinformationssystem der UHH

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oai:www.edit.fis.uni-hamburg.de:publications/5dc074f6-439d-460b-824a-19b19a8181eb