1wv1: Difference between revisions

Revision as of 01:12, 29 July 2008

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File:1wv1.png

Template:STRUCTURE 1wv1

Crystallographic studies on acyl ureas, a new class of inhibitors of glycogenphosphorylase. Broad specificity of the allosteric siteCrystallographic studies on acyl ureas, a new class of inhibitors of glycogenphosphorylase. Broad specificity of the allosteric site

Template:ABSTRACT PUBMED 15987904

About this StructureAbout this Structure

1WV1 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic studies on acyl ureas, a new class of glycogen phosphorylase inhibitors, as potential antidiabetic drugs., Oikonomakos NG, Kosmopoulou MN, Chrysina ED, Leonidas DD, Kostas ID, Wendt KU, Klabunde T, Defossa E, Protein Sci. 2005 Jul;14(7):1760-71. PMID:15987904

Acyl ureas as human liver glycogen phosphorylase inhibitors for the treatment of type 2 diabetes., 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, J Med Chem. 2005 Oct 6;48(20):6178-93. PMID:16190745

The structure of glycogen phosphorylase b with an alkyldihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor., Zographos SE, Oikonomakos NG, Tsitsanou KE, Leonidas DD, Chrysina ED, Skamnaki VT, Bischoff H, Goldmann S, Watson KA, Johnson LN, Structure. 1997 Nov 15;5(11):1413-25. PMID:9384557

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., Oikonomakos NG, Tsitsanou KE, Zographos SE, Skamnaki VT, Goldmann S, Bischoff H, Protein Sci. 1999 Oct;8(10):1930-45. PMID:10548038

Identification, synthesis, and characterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site., Kristiansen M, Andersen B, Iversen LF, Westergaard N, J Med Chem. 2004 Jul 1;47(14):3537-45. PMID:15214781

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-'''Crystallographic studies on acyl ureas, a new class of inhibitors of glycogenphosphorylase. Broad specificity of the allosteric site'''
+===Crystallographic studies on acyl ureas, a new class of inhibitors of glycogenphosphorylase. Broad specificity of the allosteric site===
-==Overview==
+<!--
-Acyl ureas were discovered as a novel class of inhibitors for glycogen phosphorylase, a molecular target to control hyperglycemia in type 2 diabetics. This series is exemplified by 6-{2,6-Dichloro- 4-[3-(2-chloro-benzoyl)-ureido]-phenoxy}-hexanoic acid, which inhibits human liver glycogen phosphorylase a with an IC(50) of 2.0 microM. Here we analyze four crystal structures of acyl urea derivatives in complex with rabbit muscle glycogen phosphorylase b to elucidate the mechanism of inhibition of these inhibitors. The structures were determined and refined to 2.26 Angstroms resolution and demonstrate that the inhibitors bind at the allosteric activator site, where the physiological activator AMP binds. Acyl ureas induce conformational changes in the vicinity of the allosteric site. Our findings suggest that acyl ureas inhibit glycogen phosphorylase by direct inhibition of AMP binding and by indirect inhibition of substrate binding through stabilization of the T' state.
+The line below this paragraph, {{ABSTRACT_PUBMED_15987904}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15987904 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15987904}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Crystallographic studies on acyl ureas, a new class of glycogen phosphorylase inhibitors, as potential antidiabetic drugs., Oikonomakos NG, Kosmopoulou MN, Chrysina ED, Leonidas DD, Kostas ID, Wendt KU, Klabunde T, Defossa E, Protein Sci. 2005 Jul;14(7):1760-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15987904 15987904]
+Acyl ureas as human liver glycogen phosphorylase inhibitors for the treatment of type 2 diabetes., 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, J Med Chem. 2005 Oct 6;48(20):6178-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16190745 16190745]
+The structure of glycogen phosphorylase b with an alkyldihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor., Zographos SE, Oikonomakos NG, Tsitsanou KE, Leonidas DD, Chrysina ED, Skamnaki VT, Bischoff H, Goldmann S, Watson KA, Johnson LN, Structure. 1997 Nov 15;5(11):1413-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9384557 9384557]
+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., Oikonomakos NG, Tsitsanou KE, Zographos SE, Skamnaki VT, Goldmann S, Bischoff H, Protein Sci. 1999 Oct;8(10):1930-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10548038 10548038]
+Identification, synthesis, and characterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site., Kristiansen M, Andersen B, Iversen LF, Westergaard N, J Med Chem. 2004 Jul 1;47(14):3537-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15214781 15214781]
 [[Category: Oryctolagus cuniculus]]
 [[Category: Phosphorylase]]
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 [[Category: Glycogenolysis]]
 [[Category: Type 2 diabetes]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:10:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:12:02 2008''