Synthesis, SAR, and X-ray structure of tricyclic compounds as potent FBPase inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 19, Issue 20, 2009, Pages 5909-5912

  Tsukada, Tomoharu ^a   Takahashi, Mizuki ^a   Takemoto, Toshiyasu ^a   Kanno, Osamu ^a   Yamane, Takahiro ^a   Kawamura, Sayako ^a   Nishi, Takahide ^a  

^a DAIICHI SANKYO CO   (Japan)

Author keywords

AMP; Fructose 1,6 bisphosphatase (FBPase); Gluconeogenesis

Indexed keywords

ADENOSINE PHOSPHATE; CS 917; ENZYME INHIBITOR; FRUCTOSE BISPHOSPHATASE; MB 05032; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; DRUG ACTIVITY; DRUG STRUCTURE; DRUG SYNTHESIS; HUMAN; IC 50; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

BENZOTHIAZOLES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; FRUCTOSE-BISPHOSPHATASE; GLUCONEOGENESIS; HETEROCYCLIC COMPOUNDS, 3-RING; HUMANS; HYDROGEN BONDING; PHOSPHONIC ACIDS; PHOSPHORIC ACID ESTERS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 70349205472     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2009.08.081     Document Type: Article

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22. The X-ray crystallographic study was accomplished according to the procedure described in Ref. 4a. Crystals of FBPase-8l complex were grown using the hanging drop vapor diffusion method at 22 °C from a protein solution (6-10 mg/mL FBPase, 20 mM Tris/HCl (pH 8.5), 1 mM DTT, 0.1 mM EDTA, 1 mM 8l) combined with an equal volume of a reservoir solution (8-10% PEG3350, 0.15 M NaCl, and 0.1 M Tris/HCl (pH 8.5)). The FBPase-8l cocrystal was diffracted to 2.6 Å in resolution and the structure was solved by the molecular replacement method with a tetramer model of the published human FBPase structure (PDB 1fta). The coordinate and statistics of FBPase-8l complex are available from the PDB using accession code 3a29.
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