Structural features of the aldose reductase and aldehyde reductase inhibitor-binding sites.
Ossama El‐Kabbani, David K. Wilson, Mark Petrash, Florante A. Quiocho
Abstract
Ossama El‐Kabbani, David K. Wilson, Mark Petrash, Florante A. Quiocho
Abstract
The three-dimensional structures of aldose reductase and aldehyde reductase, members of the aldo-keto reductase superfamily, are composed of similar alpha/beta TIM-barrels. However, examination of the structures reveals that the inhibitor-binding site of aldose reductase differs from that of aldehyde reductase due to the participation of non-conserved residues in its formation. This information will be useful in the design of inhibitors to prevent or delay diabetic retinopathy. A review of the structures of the inhibitor-binding sites is presented.
OpenAlex reports 66 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
The three-dimensional structures of aldose reductase and aldehyde reductase, members of the aldo-keto reductase superfamily, are composed of similar alpha/beta TIM-barrels. However, examination of the structures reveals that the inhibitor-binding site of aldose reductase differs from that of aldehyde reductase due to the participation of non-conserved residues in its formation. This information will be useful in the design of inhibitors to prevent or delay diabetic retinopathy. A review of the structures of the inhibitor-binding sites is presented.
Key concepts: Aldehyde Reductase, Aldose reductase, Aldose reductase inhibitor, Aldo-keto reductase, Reductase, Biochemistry, Binding site, 7-Dehydrocholesterol reductase