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Structural flexibility of the N-terminal beta-barrel domain of 15-lipoxygenase-1 probed by small angle X-ray scattering. Functional consequences for activity regulation and membrane binding


Structural flexibility of the N-terminal beta-barrel domain of 15-lipoxygenase-1 probed by small angle X-ray scattering. Functional consequences for activity regulation and membrane binding



Journal of Molecular Biology 343(4): 917-929



ISSN/ISBN: 0022-2836

PMID: 15476810

DOI: 10.1016/j.jmb.2004.08.076

Mammalian lipoxygenases form a heterogeneous family of lipid peroxidizing enzymes, which have been implicated in synthesis of inflammatory mediators, in cell development and in the pathogenesis of various diseases (atherosclerosis, osteoporosis) with major health political importance. The crystal structures of two plant lipoxygenase isoforms have been solved and X-ray coordinates for an inhibitor complex of the rabbit 15-lipoxygenase-1 are also accessible.

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Accession: 012589220

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