1n8q
From Proteopedia
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| - | [[Image:1n8q.jpg|left|200px]] | + | [[Image:1n8q.jpg|left|200px]] |
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| - | '''LIPOXYGENASE IN COMPLEX WITH PROTOCATECHUIC ACID''' | + | {{Structure |
| + | |PDB= 1n8q |SIZE=350|CAPTION= <scene name='initialview01'>1n8q</scene>, resolution 2.100Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=DHB:3,4-DIHYDROXYBENZOIC ACID'>DHB</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''LIPOXYGENASE IN COMPLEX WITH PROTOCATECHUIC ACID''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N8Q is a [ | + | 1N8Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8Q OCA]. |
==Reference== | ==Reference== | ||
| - | Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution., Borbulevych OY, Jankun J, Selman SH, Skrzypczak-Jankun E, Proteins. 2004 Jan 1;54(1):13-9. PMID:[http:// | + | Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution., Borbulevych OY, Jankun J, Selman SH, Skrzypczak-Jankun E, Proteins. 2004 Jan 1;54(1):13-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14705020 14705020] |
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: Lipoxygenase]] | [[Category: Lipoxygenase]] | ||
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[[Category: quercetin]] | [[Category: quercetin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:53:37 2008'' |
Revision as of 10:53, 20 March 2008
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| , resolution 2.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Lipoxygenase, with EC number 1.13.11.12 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LIPOXYGENASE IN COMPLEX WITH PROTOCATECHUIC ACID
Overview
PUFA metabolites have a profound effect on inflammatory diseases and cancer progression. Blocking their production by inhibiting PUFA metabolizing enzymes (dioxygenases: cyclooxygenases and LOXs) might be a successful way to control and relieve such problems, if we learn to better understand their actions at a molecular level. Compounds with strong antioxidative and free radical scavenging properties, such as polyphenols, could be effective in blocking PUFA activities, and natural flavonoids possess such qualities. Quercetin belongs to the group of natural catecholic compounds and is known as a potent, competitive inhibitor of LOX. Structural analysis reveals that quercetin entrapped within LOX undergoes degradation, and the resulting compound has been identified by X-ray analysis as protocatechuic acid (3,4-dihydroxybenzoic acid) positioned near the iron site. Its C3-OH group points toward His523, C4-OH forms a hydrogen bond with O=C from the enzyme's C-terminus, and the carboxylic group is incorporated into the hydrogen bonding network of the active-site neighborhood via Gln514. This unexpected result, together with our previous observations concerning other polyphenols, yields new evidence about the metabolism of natural flavonoids. These compounds might be vulnerable to the co-oxidase activity of LOX, leading to enzyme-stimulated oxidative degradation, which results in an inhibitor of a lower molecular weight.
About this Structure
1N8Q is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution., Borbulevych OY, Jankun J, Selman SH, Skrzypczak-Jankun E, Proteins. 2004 Jan 1;54(1):13-9. PMID:14705020
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