1wv0: Difference between revisions
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[[Image:1wv0.png|left|200px]] | [[Image:1wv0.png|left|200px]] | ||
{{STRUCTURE_1wv0| PDB=1wv0 | SCENE= }} | {{STRUCTURE_1wv0| PDB=1wv0 | SCENE= }} | ||
===Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site=== | ===Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site=== | ||
{{ABSTRACT_PUBMED_15987904}} | {{ABSTRACT_PUBMED_15987904}} | ||
==About this Structure== | ==About this Structure== | ||
[[1wv0]] 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=1WV0 OCA]. | [[1wv0]] is a 1 chain structure of [[Glycogen Phosphorylase]] 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=1WV0 OCA]. | ||
==See Also== | |||
*[[Glycogen Phosphorylase|Glycogen Phosphorylase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:015987904</ref><ref group="xtra">PMID:016190745</ref><ref group="xtra">PMID:009384557</ref><ref group="xtra">PMID:010548038</ref><ref group="xtra">PMID:015214781</ref><references group="xtra"/> | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Phosphorylase]] | [[Category: Phosphorylase]] | ||
Revision as of 16:04, 25 July 2012
Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric siteCrystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site
Template:ABSTRACT PUBMED 15987904
About this StructureAbout this Structure
1wv0 is a 1 chain structure of Glycogen Phosphorylase with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5]
- ↑ Oikonomakos NG, Kosmopoulou MN, Chrysina ED, Leonidas DD, Kostas ID, Wendt KU, Klabunde T, Defossa E. Crystallographic studies on acyl ureas, a new class of glycogen phosphorylase inhibitors, as potential antidiabetic drugs. Protein Sci. 2005 Jul;14(7):1760-71. PMID:15987904 doi:14/7/1760
- ↑ Klabunde T, Wendt KU, Kadereit D, Brachvogel V, Burger HJ, Herling AW, Oikonomakos NG, Kosmopoulou MN, Schmoll D, Sarubbi E, von Roedern E, Schonafinger K, Defossa E. Acyl ureas as human liver glycogen phosphorylase inhibitors for the treatment of type 2 diabetes. J Med Chem. 2005 Oct 6;48(20):6178-93. PMID:16190745 doi:10.1021/jm049034y
- ↑ Zographos SE, Oikonomakos NG, Tsitsanou KE, Leonidas DD, Chrysina ED, Skamnaki VT, Bischoff H, Goldmann S, Watson KA, Johnson LN. The structure of glycogen phosphorylase b with an alkyldihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor. Structure. 1997 Nov 15;5(11):1413-25. PMID:9384557
- ↑ Oikonomakos NG, Tsitsanou KE, Zographos SE, Skamnaki VT, Goldmann S, Bischoff H. Allosteric inhibition of glycogen phosphorylase a by the potential antidiabetic drug 3-isopropyl 4-(2-chlorophenyl)-1,4-dihydro-1-ethyl-2-methyl-pyridine-3,5,6-tricarbo xylate. Protein Sci. 1999 Oct;8(10):1930-45. PMID:10548038
- ↑ Kristiansen M, Andersen B, Iversen LF, Westergaard N. Identification, synthesis, and characterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site. J Med Chem. 2004 Jul 1;47(14):3537-45. PMID:15214781 doi:10.1021/jm031121n