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1lox

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[[Image:1lox.gif|left|200px]]
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{{STRUCTURE_1lox| PDB=1lox | SCENE= }}
{{STRUCTURE_1lox| PDB=1lox | SCENE= }}
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'''RABBIT RETICULOCYTE 15-LIPOXYGENASE'''
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===RABBIT RETICULOCYTE 15-LIPOXYGENASE===
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==Overview==
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Here we report the first structure of a mammalian 15-lipoxygenase. The protein is composed of two domains; a catalytic domain and a previously unrecognized beta-barrel domain. The N-terminal beta-barrel domain has topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within the C-terminal domain, the lipoxygenase substrate binding site is a hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be docked into this deep hydrophobic pocket with the methyl end extending down into the bottom of the pocket and the acid end tethered by a conserved basic residue on the surface of the enzyme. This structure provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.
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(as it appears on PubMed at http://www.pubmed.gov), where 9406550 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9406550}}
==About this Structure==
==About this Structure==
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[[Category: 15lo_depot2]]
[[Category: 15lo_depot2]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:07:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:39:53 2008''

Revision as of 18:39, 2 July 2008

Image:1lox.png

Template:STRUCTURE 1lox

RABBIT RETICULOCYTE 15-LIPOXYGENASE

Template:ABSTRACT PUBMED 9406550

About this Structure

1LOX is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:9406550

Page seeded by OCA on Wed Jul 2 21:39:53 2008

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