Crystal structure of 12-Lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis

Structure

Volumn 20, Issue 9, 2012, Pages 1490-1497

  Xu, Shu ^a   Mueser, Timothy C ^a   Marnett, Lawrence J ^b   Funk Jr , Max O ^a  

^a UNIVERSITY OF TOLEDO   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 (2 OXAPENTADECA 4 YNE)PHENYLPROPANOIC ACID; ARACHIDONATE 12 LIPOXYGENASE; ARACHIDONIC ACID; IRON; LIPOXYGENASE INHIBITOR; OXYGEN; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; CHANNEL GATING; CHEMICAL REACTION; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ANIMALS; ARACHIDONATE 12-LIPOXYGENASE; BIOCATALYSIS; CATALYTIC DOMAIN; COORDINATION COMPLEXES; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; IRON; LIPOXYGENASE INHIBITORS; MODELS, MOLECULAR; OXYGEN; PHENYLPROPIONATES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SUS SCROFA;

EID: 84865800398     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.06.003     Document Type: Article

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