1az2

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Revision as of 22:27, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1az2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1az2, resolution 2.9Å" /> '''CITRATE BOUND, C298A...)
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File:1az2.gif


1az2, resolution 2.9Å

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CITRATE BOUND, C298A/W219Y MUTANT HUMAN ALDOSE REDUCTASE

OverviewOverview

It is generally expected that only one inhibitor molecule will bind to an, enzyme active site. In fact, specific drug design theories depend upon, this assumption. Here, we report the binding of two molecules of an, inhibitor to the same active site which we observed in the 1.8 A, resolution structure of the drug Alrestatin bound to a mutant of human, aldose reductase. The two molecules of Alrestatin bind to the active site, in a stacked arrangement (a double-decker). This stack positions the, carboxylic acid of one drug molecule near the NADP+ cofactor at a, previously determined anion binding site and the carboxylic acid of the, second drug molecule near the carboxy-terminal tail of the enzyme. We, propose that interactions of inhibitors with the carboxy-terminal loop of, aldose ... [(full description)]

About this StructureAbout this Structure

1AZ2 is a [Single protein] structure of sequence from [Homo sapiens] with NAP and CIT as [ligands]. Active as [[1]], with EC number [1.1.1.21]. Full crystallographic information is available from [OCA].

ReferenceReference

The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant., Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH, Biochemistry. 1997 Dec 23;36(51):16134-40. PMID:9405046

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