2ffr: Difference between revisions
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[[Image:2ffr.png|left|200px]] | [[Image:2ffr.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
[[2ffr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FFR OCA]. | |||
==Reference== | ==Reference== | ||
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[[Category: Glycogenolysis]] | [[Category: Glycogenolysis]] | ||
[[Category: Inhibition]] | [[Category: Inhibition]] | ||
[[Category: Transferase]] | |||
[[Category: Type 2 diabetes]] | [[Category: Type 2 diabetes]] | ||
Revision as of 03:02, 15 March 2011
Crystallographic studies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamineCrystallographic studies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine
Template:ABSTRACT PUBMED 16616506
About this StructureAbout this Structure
2ffr is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Petsalakis EI, Chrysina ED, Tiraidis C, Hadjiloi T, Leonidas DD, Oikonomakos NG, Aich U, Varghese B, Loganathan D. Crystallographic studies on N-azidoacetyl-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine. Bioorg Med Chem. 2006 Aug 1;14(15):5316-24. Epub 2006 Apr 17. PMID:16616506 doi:10.1016/j.bmc.2006.03.044
- ↑ Anagnostou E, Kosmopoulou MN, Chrysina ED, Leonidas DD, Hadjiloi T, Tiraidis C, Zographos SE, Gyorgydeak Z, Somsak L, Docsa T, Gergely P, Kolisis FN, Oikonomakos NG. Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-D-glucopyranosylamine and N-trifluoroacetyl-beta-D-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase. Bioorg Med Chem. 2006 Jan 1;14(1):181-9. Epub 2005 Oct 4. PMID:16213146 doi:10.1016/j.bmc.2005.08.010