2fhy: Difference between revisions

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New page: left|200px<br /> <applet load="2fhy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fhy, resolution 2.95Å" /> '''Structure of human ...
 
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[[Image:2fhy.gif|left|200px]]<br />
<applet load="2fhy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2fhy, resolution 2.95&Aring;" />
'''Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor'''<br />


==Overview==
==Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor==
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.
<StructureSection load='2fhy' size='340' side='right'caption='[[2fhy]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==Disease==
==See Also==
Known disease associated with this structure: Fructose-bisphosphatase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=229700 229700]]
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
 
== References ==
==About this Structure==
<references/>
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 MG and A37 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FHY OCA].
__TOC__
 
</StructureSection>
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: A37]]
[[Category: MG]]
[[Category: allosteric inhibitors human fbpase]]
[[Category: benzoxazole]]
[[Category: intersubunit allosteric inhibition of human fpbase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:05:36 2007''

Latest revision as of 09:23, 14 February 2024

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

2fhy, resolution 2.95Å

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