1lox: Difference between revisions

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[[Image:1lox.gif|left|200px]]
{{Seed}}
[[Image:1lox.png|left|200px]]


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{{STRUCTURE_1lox|  PDB=1lox  |  SCENE=  }}  
{{STRUCTURE_1lox|  PDB=1lox  |  SCENE=  }}  


'''RABBIT RETICULOCYTE 15-LIPOXYGENASE'''
===RABBIT RETICULOCYTE 15-LIPOXYGENASE===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_9406550}}, adds the Publication Abstract to the page
(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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