2JJK: Fructose-1,6-Bisphosphatase(D-Fructose-1,6-Bisphosphate -1-Phosphohydrolase) (E.C.3.1.3.11) Complexed With A Dual Binding Amp Site Inhibitor

Citation:
Abstract
Human fructose-1,6-bisphosphatase (FBPase, EC 3.1.3.11) is a key gluconeogenic enzyme, responsible for the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate, and thus presents an opportunity for the development of novel therapeutics focused on lowering the hepatic glucose production in type 2 diabetics. In its active form FBPase exists as a homotetramer and is allosterically regulated by AMP. In an HTS campaign aromatic sulfonylureas have been identified as FBPase inhibitors mimicking AMP. By bridging two adjacent allosteric binding sites using two aromatic sulfonylureas as anchor units and covalently linking them, it was possible to obtain dual binding AMP site inhibitors that exhibit a strong inhibitory effect.
PDB ID: 2JJKDownload
MMDB ID: 65534
PDB Deposition Date: 2008/4/9
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 2JJK: tetrameric; determined by author and by software (PQS)
Molecular Components in 2JJK
Label Count Molecule
Proteins (4 molecules)
4
Fructose-1,6-bisphosphatase 1(Gene symbol: FBP1)
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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