1h35: Difference between revisions

Revision as of 06:32, 1 July 2008

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File:1h35.png

Template:STRUCTURE 1h35

STRUCTURES OF HUMAN OXIDOSQUALENE CYCLASE INHIBITORS BOUND TO A HOMOLGOUS ENZYMESTRUCTURES OF HUMAN OXIDOSQUALENE CYCLASE INHIBITORS BOUND TO A HOMOLGOUS ENZYME

Template:ABSTRACT PUBMED 12747780

About this StructureAbout this Structure

1H35 is a Single protein structure of sequence from Alicyclobacillus acidocaldarius. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''STRUCTURES OF HUMAN OXIDOSQUALENE CYCLASE INHIBITORS BOUND TO A HOMOLGOUS ENZYME'''
+===STRUCTURES OF HUMAN OXIDOSQUALENE CYCLASE INHIBITORS BOUND TO A HOMOLGOUS ENZYME===
-==Overview==
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-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.
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 [[Category: Monotopic membrane]]
 [[Category: Oxidosqualene cyclase]]
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