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2fhy

From Proteopedia

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[[Image:2fhy.gif|left|200px]]<br /><applet load="2fhy" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fhy, resolution 2.95&Aring;" />
 
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'''Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor'''<br />
 
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==Overview==
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==Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor==
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We have identified benzoxazole benzenesulfonamide 1 as a novel allosteric inhibitor of fructose-1,6-bisphosphatase (FBPase-1). X-ray crystallographic and biological studies of 1 indicate a distinct binding mode that recapitulates features of several previously reported FBPase-1 inhibitor classes.
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<StructureSection load='2fhy' size='340' side='right'caption='[[2fhy]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fhy]] is a 4 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=2FHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FHY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A37:2,5-DICHLORO-N-(5-CHLORO-1,3-BENZOXAZOL-2-YL)BENZENESULFONAMIDE'>A37</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fhy OCA], [https://pdbe.org/2fhy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fhy RCSB], [https://www.ebi.ac.uk/pdbsum/2fhy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fhy ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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>
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== Function ==
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[https://www.uniprot.org/uniprot/F16P1_HUMAN F16P1_HUMAN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/2fhy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fhy ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Fructose-1,6-bidphosphatase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611570 611570]]
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*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2FHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=A37:'>A37</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHY OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Benzoxazole benzenesulfonamides are novel allosteric inhibitors of fructose-1,6-bisphosphatase with a distinct binding mode., von Geldern TW, Lai C, Gum RJ, Daly M, Sun C, Fry EH, Abad-Zapatero C, Bioorg Med Chem Lett. 2006 Apr 1;16(7):1811-5. Epub 2006 Jan 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16442285 16442285]
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[[Category: Fructose-bisphosphatase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Abad-Zapatero, C.]]
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[[Category: Abad-Zapatero C]]
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[[Category: A37]]
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[[Category: MG]]
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[[Category: allosteric inhibitors human fbpase]]
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[[Category: benzoxazole]]
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[[Category: intersubunit allosteric inhibition of human fpbase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:36 2008''
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Current revision

Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor

PDB ID 2fhy

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