3tu9 | pdb_00003tu9
From Proteopedia
Crystal structure of rabbit muscle aldolase bound with 5-O-methyl mannitol 1,6-phosphate
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Structural highlights
Function[ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1] Publication Abstract from PubMedSeveral 5-O-alkyl- and 5-C-alkyl-mannitol bis-phosphates were synthesized and comparatively assayed as inhibitors of fructose bis-phosphate aldolases (Fbas) from rabbit muscle (taken as surrogate model of the human enzyme) and from Trypanosoma brucei. A limited selectivity was found in several instances. Crystallographic studies confirm that the 5-O-methyl derivative binds competitively with substrate and the 5-O-methyl moiety penetrating deeper into a shallow hydrophobic pocket at the active site. This observation can lead to the preparation of selective competitive or irreversible inhibitors of the parasite Fba. Mannitol Bis-phosphate Based Inhibitors of Fructose 1,6-Bisphosphate Aldolases.,Mabiala-Bassiloua CG, Arthus-Cartier G, Hannaert V, Therisod H, Sygusch J, Therisod M ACS Med Chem Lett. 2011 Sep 3;2(11):804-8. doi: 10.1021/ml200129s. eCollection, 2011 Nov 10. PMID:24900268[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 06:06, 18 April 2018.