4NRE
The structure of human 15-lipoxygenase-2 with a substrate mimic
Summary for 4NRE
| Entry DOI | 10.2210/pdb4nre/pdb |
| Descriptor | Arachidonate 15-lipoxygenase B, FE (II) ION, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (7 entities in total) |
| Functional Keywords | calcium binding, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform A: Nucleus. Cytoplasm, cytosol: O15296 |
| Total number of polymer chains | 1 |
| Total formula weight | 80282.80 |
| Authors | Kobe, M.J.,Neau, D.B.,Mitchell, C.E.,Bartlett, S.G.,Newcomer, M.E. (deposition date: 2013-11-26, release date: 2014-02-12, Last modification date: 2024-02-28) |
| Primary citation | Kobe, M.J.,Neau, D.B.,Mitchell, C.E.,Bartlett, S.G.,Newcomer, M.E. The structure of human 15-lipoxygenase-2 with a substrate mimic. J.Biol.Chem., 289:8562-8569, 2014 Cited by PubMed Abstract: Atherosclerosis is associated with chronic inflammation occurring over decades. The enzyme 15-lipoxygenase-2 (15-LOX-2) is highly expressed in large atherosclerotic plaques, and its activity has been linked to the progression of macrophages to the lipid-laden foam cells present in atherosclerotic plaques. We report here the crystal structure of human 15-LOX-2 in complex with an inhibitor that appears to bind as a substrate mimic. 15-LOX-2 contains a long loop, composed of hydrophobic amino acids, which projects from the amino-terminal membrane-binding domain. The loop is flanked by two Ca(2+)-binding sites that confer Ca(2+)-dependent membrane binding. A comparison of the human 15-LOX-2 and 5-LOX structures reveals similarities at the active sites, as well striking differences that can be exploited for design of isoform-selective inhibitors. PubMed: 24497644DOI: 10.1074/jbc.M113.543777 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.63 Å) |
Structure validation
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