1hu9
From Proteopedia
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| , resolution 2.2Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Lipoxygenase, with EC number 1.13.11.12 | ||||||
| Related: | 1LNH, 1BYT, 1YGE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH 4-HYDROPEROXY-2-METHOXY-PHENOL
Overview
Scientific research provides documented evidence that fatty acid metabolites have profound impact on carcinogenesis. Intervention into dioxygenase pathways might therefore effect development, metastasis and progression of many types of cancers. This work delivers the first 3D structural data and explains how curcumin interacts with the fatty acid metabolizing enzyme, soybean lipoxygenase. Curcumin binds to lipoxygenase in a non-competitive manner. Trapped in that complex, it undergoes photodegradation in the X-rays, but utilizes enzyme catalytic ability to form the peroxy complex Enz-Fe-O-O-R as 4-hydroperoxy-2-methoxy-phenol, that later transforms into 2-methoxycyclohexa-2,5-diene-1,4-dione. Our observations about this radiation and time-dependent inhibition add new information to the role that curcumin might play in cancer prevention and treatment.
About this Structure
1HU9 is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Structure of curcumin in complex with lipoxygenase and its significance in cancer., Skrzypczak-Jankun E, Zhou K, McCabe NP, Selman SH, Jankun J, Int J Mol Med. 2003 Jul;12(1):17-24. PMID:12792803
Page seeded by OCA on Sun Mar 30 21:10:29 2008
