2x24

bovine ACC2 CT domain in complex with inhibitorbovine ACC2 CT domain in complex with inhibitor

Structural highlights 2x24 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Inhibition of acetyl-CoA carboxylases has the potential for modulating long chain fatty acid biosynthesis and mitochondrial fatty acid oxidation. Hybridization of weak inhibitors of ACC2 provided a novel, moderately potent but lipophilic series. Optimization led to compounds 33 and 37, which exhibit potent inhibition of human ACC2, 10-fold selectivity over inhibition of human ACC1, good physical and in vitro ADME properties and good bioavailability. X-ray crystallography has shown this series binding in the CT-domain of ACC2 and revealed two key hydrogen bonding interactions. Both 33 and 37 lower levels of hepatic malonyl-CoA in vivo in obese Zucker rats. Design of small molecule inhibitors of acetyl-CoA carboxylase 1 and 2 showing reduction of hepatic malonyl-CoA levels in vivo in obese Zucker rats.,Bengtsson C, Blaho S, Saitton DB, Brickmann K, Broddefalk J, Davidsson O, Drmota T, Folmer R, Hallberg K, Hallen S, Hovland R, Isin E, Johannesson P, Kull B, Larsson LO, Lofgren L, Nilsson KE, Noeske T, Oakes N, Plowright AT, Schnecke V, Stahlberg P, Sorme P, Wan H, Wellner E, Oster L Bioorg Med Chem. 2011 May 15;19(10):3039-53. Epub 2011 Apr 13. PMID:21515056 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acetyl-CoA carboxylase 3D structures

spinqualitylabelsall models 2x24, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image