2wbd

From Proteopedia

(Difference between revisions)

Current revision

FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR

Structural highlights

2wbd is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

F16P1_HUMAN Defects in FBP1 are the cause of fructose-1,6-bisphosphatase deficiency (FBPD) [MIM:229700. FBPD is inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis (lactacidemia) in newborn infants or young children.^[1] ^[2]

Function

F16P1_HUMAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Sulfonylureido thiazoles were identified from a HTS campaign and optimized through a combination of structure-activity studies, X-ray crystallography and molecular modeling to yield potent inhibitors of fructose-1,6-bisphosphatase. Compound 12 showed favorable ADME properties, for example, F=70%, and a robust 32% glucose reduction in the acute db/db mouse model for Type-2 diabetes.

Sulfonylureido thiazoles as fructose-1,6-bisphosphatase inhibitors for the treatment of type-2 diabetes.,Kitas E, Mohr P, Kuhn B, Hebeisen P, Wessel HP, Haap W, Ruf A, Benz J, Joseph C, Huber W, Sanchez RA, Paehler A, Benardeau A, Gubler M, Schott B, Tozzo E Bioorg Med Chem Lett. 2010 Jan 15;20(2):594-9. Epub 2009 Nov 22. PMID:19969452^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kikawa Y, Inuzuka M, Jin BY, Kaji S, Koga J, Yamamoto Y, Fujisawa K, Hata I, Nakai A, Shigematsu Y, Mizunuma H, Taketo A, Mayumi M, Sudo M. Identification of genetic mutations in Japanese patients with fructose-1,6-bisphosphatase deficiency. Am J Hum Genet. 1997 Oct;61(4):852-61. PMID:9382095
↑ Matsuura T, Chinen Y, Arashiro R, Katsuren K, Tamura T, Hyakuna N, Ohta T. Two newly identified genomic mutations in a Japanese female patient with fructose-1,6-bisphosphatase (FBPase) deficiency. Mol Genet Metab. 2002 Jul;76(3):207-10. PMID:12126934
↑ Kitas E, Mohr P, Kuhn B, Hebeisen P, Wessel HP, Haap W, Ruf A, Benz J, Joseph C, Huber W, Sanchez RA, Paehler A, Benardeau A, Gubler M, Schott B, Tozzo E. Sulfonylureido thiazoles as fructose-1,6-bisphosphatase inhibitors for the treatment of type-2 diabetes. Bioorg Med Chem Lett. 2010 Jan 15;20(2):594-9. Epub 2009 Nov 22. PMID:19969452 doi:10.1016/j.bmcl.2009.11.093

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wbd"

@@ Line 1: / Line 1: @@
-==FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1-PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR==
-<StructureSection load='2wbd' size='340' side='right' caption='[[2wbd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+==FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR==
+<StructureSection load='2wbd' size='340' side='right'caption='[[2wbd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wbd]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WBD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wbd]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WBD FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RO5:N-[(5-BROMO-1,3-THIAZOL-2-YL)CARBAMOYL]-3-ETHYLBENZENESULFONAMIDE'>RO5</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fta|1fta]], [[2jjk|2jjk]], [[2vt5|2vt5]], [[2fie|2fie]], [[2wbb|2wbb]], [[2fhy|2fhy]], [[2fix|2fix]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RO5:N-[(5-BROMO-1,3-THIAZOL-2-YL)CARBAMOYL]-3-ETHYLBENZENESULFONAMIDE'>RO5</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbd OCA], [https://pdbe.org/2wbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wbd RCSB], [https://www.ebi.ac.uk/pdbsum/2wbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wbd ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbd OCA], [http://pdbe.org/2wbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wbd RCSB], [http://www.ebi.ac.uk/pdbsum/2wbd PDBsum]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/F16P1_HUMAN F16P1_HUMAN]] Defects in FBP1 are the cause of fructose-1,6-bisphosphatase deficiency (FBPD) [MIM:[http://omim.org/entry/229700 229700]]. FBPD is inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis (lactacidemia) in newborn infants or young children.<ref>PMID:9382095</ref> <ref>PMID:12126934</ref>
+[https://www.uniprot.org/uniprot/F16P1_HUMAN F16P1_HUMAN] Defects in FBP1 are the cause of fructose-1,6-bisphosphatase deficiency (FBPD) [MIM:[https://omim.org/entry/229700 229700]. FBPD is inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis (lactacidemia) in newborn infants or young children.<ref>PMID:9382095</ref> <ref>PMID:12126934</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/F16P1_HUMAN F16P1_HUMAN]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wb/2wbd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wb/2wbd_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 33: @@
 ==See Also==
-*[[Fructose-1%2C6-bisphosphatase|Fructose-1%2C6-bisphosphatase]]
+*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Fructose-bisphosphatase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Benz, J]]
+[[Category: Alvarez Sanchez R]]
-[[Category: Bernadeau, A]]
+[[Category: Benz J]]
-[[Category: Fol, B]]
+[[Category: Bernadeau A]]
-[[Category: Gubler, M]]
+[[Category: Fol B]]
-[[Category: Haap, W]]
+[[Category: Gubler M]]
-[[Category: Hebeisen, P]]
+[[Category: Haap W]]
-[[Category: Huber, W]]
+[[Category: Hebeisen P]]
-[[Category: Joseph, C]]
+[[Category: Huber W]]
-[[Category: Kitas, E]]
+[[Category: Joseph C]]
-[[Category: Kuhn, B]]
+[[Category: Kitas E]]
-[[Category: Mohr, P]]
+[[Category: Kuhn B]]
-[[Category: Paehler, A]]
+[[Category: Mohr P]]
-[[Category: Ruf, A]]
+[[Category: Paehler A]]
-[[Category: Sanchez, R Alvarez]]
+[[Category: Ruf A]]
-[[Category: Schott, B]]
+[[Category: Schott B]]
-[[Category: Tetaz, T]]
+[[Category: Tetaz T]]
-[[Category: Tozzo, E]]
+[[Category: Tozzo E]]
-[[Category: Wessel, H P]]
+[[Category: Wessel HP]]
-[[Category: Allosteric enzyme]]
-[[Category: Carbohydrate metabolism]]
-[[Category: Gluconeogenesis]]
-[[Category: Hydrolase]]
-[[Category: Phosphoric monoester]]

2wbd

From Proteopedia

Current revision

FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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