Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data

Proteins: Structure, Function and Genetics

Volumn 70, Issue 3, 2008, Pages 1023-1032

  Choi, Jongkeun ^a   Jae, Kyung Chon ^a   Kim, Sangsoo ^b   Shin, Whanchul ^a  

^a Seoul National University   (South Korea)

^b Soongsil University   (South Korea)

Author keywords

Arachidonate binding mode; Crystal structure; Crystal twinning; Ligand induced conformational change; Pseudo symmetry

Indexed keywords

ARACHIDONATE 15 LIPOXYGENASE; FATTY ACID; HEME; HEME OXYGENASE; LIPOXYGENASE;

ALPHA HELIX; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; RABBIT; STEREOCHEMISTRY; STEREOSPECIFICITY;

ANIMALS; ARACHIDONATE 15-LIPOXYGENASE; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DATABASES, PROTEIN; HUMANS; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

MAMMALIA; ORYCTOLAGUS CUNICULUS;

EID: 38549129314     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21590     Document Type: Article

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