1h36: Difference between revisions

Latest revision as of 08:52, 9 May 2024

Structures of Human Oxidosqualene Cyclase Inhibitors Bound to an Homologous Enzyme

Structural highlights

1h36 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 2.8Å
Ligands:	C8E, R88
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.

References

↑ 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:https://dx.doi.org/10.1021/jm0211218

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OCA

[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:https://dx.doi.org/10.1021/jm0211218

[1]

@@ Line 1: / Line 1: @@
-==Structures of human oxidosqualene cyclase inhibitors bound to a homolgous enzyme==
+==Structures of Human Oxidosqualene Cyclase Inhibitors Bound to an Homologous Enzyme==
-<StructureSection load='1h36' size='340' side='right' caption='[[1h36]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='1h36' size='340' side='right'caption='[[1h36]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h36]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27009 Atcc 27009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H36 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h36]] 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=1H36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H36 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=R88:(4-BROMOPHENYL)[4-({(2E)-4-[CYCLOPROPYL(METHYL)AMINO]BUT-2-ENYL}OXY)PHENYL]METHANONE'>R88</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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gsz|1gsz]], [[1h35|1h35]], [[1h37|1h37]], [[1h39|1h39]], [[1h3a|1h3a]], [[1h3b|1h3b]], [[1h3c|1h3c]], [[1sqc|1sqc]], [[2sqc|2sqc]], [[3sqc|3sqc]]</td></tr>
+<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=R88:(4-BROMOPHENYL)[4-({(2E)-4-[CYCLOPROPYL(METHYL)AMINO]BUT-2-ENYL}OXY)PHENYL]METHANONE'>R88</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Squalene--hopene_cyclase Squalene--hopene cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.17 5.4.99.17] </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=1h36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h36 OCA], [https://pdbe.org/1h36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h36 RCSB], [https://www.ebi.ac.uk/pdbsum/1h36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h36 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=1h36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h36 OCA], [http://pdbe.org/1h36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h36 RCSB], [http://www.ebi.ac.uk/pdbsum/1h36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h36 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]]
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1h36" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Squalene-hopene cyclase|Squalene-hopene cyclase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 27009]]
+[[Category: Alicyclobacillus acidocaldarius]]
-[[Category: Squalene--hopene cyclase]]
+[[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: Cholesterol biosynthesis]]
-[[Category: Inhibitor]]
-[[Category: Isomerase]]
-[[Category: Monotopic membrane protein]]

1h36: Difference between revisions

Latest revision as of 08:52, 9 May 2024

Structures of Human Oxidosqualene Cyclase Inhibitors Bound to an Homologous Enzyme

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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