2fhy: Difference between revisions

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[[Image:2fhy.gif|left|200px]]


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==Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor==
The line below this paragraph, containing "STRUCTURE_2fhy", creates the "Structure Box" on the page.
<StructureSection load='2fhy' size='340' side='right'caption='[[2fhy]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
-->
<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>
{{STRUCTURE_2fhy| PDB=2fhy |  SCENE= }}
<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>
</table>
== Disease ==
[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/fh/2fhy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


'''Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor'''
==See Also==
 
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
2FHY is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/16442285 16442285]
[[Category: Fructose-bisphosphatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abad-Zapatero, C.]]
[[Category: Abad-Zapatero C]]
[[Category: Allosteric inhibitors human fbpase]]
[[Category: Benzoxazole]]
[[Category: Intersubunit allosteric inhibition of human fpbase]]
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