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[[Image:1o6r.jpg|left|200px]]


{{Structure
==Structures of human oxidosqualene cyclase inhibitors bound to an homologous enzyme==
|PDB= 1o6r |SIZE=350|CAPTION= <scene name='initialview01'>1o6r</scene>, resolution 2.7&Aring;
<StructureSection load='1o6r' size='340' side='right'caption='[[1o6r]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
|SITE= <scene name='pdbsite=C8A:R19+Binding+Site+For+Chain+C'>C8A</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> and <scene name='pdbligand=R19:ALLYL-{6-[3-(4-BROMO-PHENYL)-BENZOFURAN-6-YLOXY]-HEXYL-}-METHYL-AMIN'>R19</scene>
<table><tr><td colspan='2'>[[1o6r]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6R FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=R19:ALLYL-{6-[3-(4-BROMO-PHENYL)-BENZOFURAN-6-YLOXY]-HEXYL-}-METHYL-AMIN'>R19</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=1o6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6r OCA], [https://pdbe.org/1o6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6r RCSB], [https://www.ebi.ac.uk/pdbsum/1o6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6r ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SQHC_ALIAD SQHC_ALIAD] Catalyzes the cyclization of squalene into hopene.
== 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/o6/1o6r_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=1o6r ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The binding structures of 11 human oxidosqualene cyclase inhibitors designed as cholesterol-lowering agents were determined for the squalene-hopene cyclase from Alicyclobacillus acidocaldarius, which is the only structurally known homologue of the human enzyme. The complexes were produced by cocrystallization, and the structures were elucidated by X-ray diffraction analyses. All inhibitors were bound in the large active center cavity. The detailed binding structures are presented and discussed in the light of the IC50 values of these 11 as well as 17 other inhibitors. They provide a consistent picture for the inhibition of the bacterial enzyme and can be used to adjust and improve homology models of the human enzyme. The detailed active center structures of the two enzymes are too different to show an IC50 correlation.


'''STRUCTURES OF HUMAN OXIDOSQUALENE CYCLASE INHIBITORS BOUND TO A HOMOLGOUS ENZYME'''
Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase.,Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE J Med Chem. 2003 May 22;46(11):2083-92. PMID:12747780<ref>PMID:12747780</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1o6r" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The binding structures of 11 human oxidosqualene cyclase inhibitors designed as cholesterol-lowering agents were determined for the squalene-hopene cyclase from Alicyclobacillus acidocaldarius, which is the only structurally known homologue of the human enzyme. The complexes were produced by cocrystallization, and the structures were elucidated by X-ray diffraction analyses. All inhibitors were bound in the large active center cavity. The detailed binding structures are presented and discussed in the light of the IC50 values of these 11 as well as 17 other inhibitors. They provide a consistent picture for the inhibition of the bacterial enzyme and can be used to adjust and improve homology models of the human enzyme. The detailed active center structures of the two enzymes are too different to show an IC50 correlation.
*[[Squalene-hopene cyclase|Squalene-hopene cyclase]]
 
== References ==
==About this Structure==
<references/>
1O6R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6R OCA].
__TOC__
 
</StructureSection>
==Reference==
Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase., Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE, J Med Chem. 2003 May 22;46(11):2083-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12747780 12747780]
[[Category: Alicyclobacillus acidocaldarius]]
[[Category: Alicyclobacillus acidocaldarius]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aebi, J D.]]
[[Category: Aebi JD]]
[[Category: Dehmlow, H.]]
[[Category: Dehmlow H]]
[[Category: Lenhart, A.]]
[[Category: Lenhart A]]
[[Category: Morand, O H.]]
[[Category: Morand OH]]
[[Category: Reinert, D J.]]
[[Category: Reinert DJ]]
[[Category: Schulz, G E.]]
[[Category: Schulz GE]]
[[Category: Weihofen, W A.]]
[[Category: Weihofen WA]]
[[Category: C8E]]
[[Category: R19]]
[[Category: cholesterol biosynthesis]]
[[Category: inhibitor]]
[[Category: interaction]]
[[Category: isomerase]]
[[Category: monotopic membrane protein]]
[[Category: oxidosqualene cyclase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:31 2008''

Latest revision as of 11:57, 9 May 2024

Structures of human oxidosqualene cyclase inhibitors bound to an homologous enzymeStructures of human oxidosqualene cyclase inhibitors bound to an homologous enzyme

Structural highlights

1o6r is a 3 chain structure with sequence from Alicyclobacillus acidocaldarius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SQHC_ALIAD Catalyzes the cyclization of squalene into hopene.

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

The binding structures of 11 human oxidosqualene cyclase inhibitors designed as cholesterol-lowering agents were determined for the squalene-hopene cyclase from Alicyclobacillus acidocaldarius, which is the only structurally known homologue of the human enzyme. The complexes were produced by cocrystallization, and the structures were elucidated by X-ray diffraction analyses. All inhibitors were bound in the large active center cavity. The detailed binding structures are presented and discussed in the light of the IC50 values of these 11 as well as 17 other inhibitors. They provide a consistent picture for the inhibition of the bacterial enzyme and can be used to adjust and improve homology models of the human enzyme. The detailed active center structures of the two enzymes are too different to show an IC50 correlation.

Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase.,Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE J Med Chem. 2003 May 22;46(11):2083-92. PMID:12747780[1]

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

See Also

References

  1. ↑ Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE. Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase. J Med Chem. 2003 May 22;46(11):2083-92. PMID:12747780 doi:http://dx.doi.org/10.1021/jm0211218

1o6r, resolution 2.70Å

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