1sg0

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(New page: 200px<br /> <applet load="1sg0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sg0, resolution 1.50&Aring;" /> '''Crystal structure a...)
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Revision as of 17:06, 12 November 2007

Image:1sg0.gif

1sg0, resolution 1.50Å

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Crystal structure analysis of QR2 in complex with resveratrol

Overview

Resveratrol has been shown to have chemopreventive, cardioprotective, and, antiaging properties. Here, we report that resveratrol is a potent, inhibitor of quinone reductase 2 (QR2) activity in vitro with a, dissociation constant of 35 nM and show that it specifically binds to the, deep active-site cleft of QR2 using high-resolution structural analysis., All three resveratrol hydroxyl groups form hydrogen bonds with amino acids, from QR2, anchoring a flat resveratrol molecule in parallel with the, isoalloxazine ring of FAD. The unique active-site pocket in QR2 could, potentially bind other natural polyphenols such as flavonoids, as proven, by the high affinity exhibited by quercetin toward QR2. K562 cells with, QR2 expression suppressed by RNAi showed similar properties as, resveratrol-treated cells in their resistance to quinone toxicity., Furthermore, the QR2 knockdown K562 cells exhibit increased antioxidant, and detoxification enzyme expression and reduced proliferation rates., These observations could imply that the chemopreventive and, cardioprotective properties of resveratrol are possibly the results of QR2, activity inhibition, which in turn, up-regulates the expression of, cellular antioxidant enzymes and cellular resistance to oxidative stress.

About this Structure

1SG0 is a Single protein structure of sequence from Homo sapiens with ZN, FAD and STL as ligands. Active as NAD(P)H dehydrogenase (quinone), with EC number 1.6.5.2 Full crystallographic information is available from OCA.

Reference

Crystal structure of quinone reductase 2 in complex with resveratrol., Buryanovskyy L, Fu Y, Boyd M, Ma Y, Hsieh TC, Wu JM, Zhang Z, Biochemistry. 2004 Sep 14;43(36):11417-26. PMID:15350128

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