2Q7R
Crystal structure of human FLAP with an iodinated analog of MK-591
Summary for 2Q7R
| Entry DOI | 10.2210/pdb2q7r/pdb |
| Related | 2q7m |
| Descriptor | Arachidonate 5-lipoxygenase-activating protein, 3-[3-(3,3-DIMETHYLBUTANOYL)-1-(4-IODOBENZYL)-5-(QUINOLIN-2-YLMETHOXY)-1H-INDOL-2-YL]-2,2-DIMETHYLPROPANOIC ACID (2 entities in total) |
| Functional Keywords | flap, mapeg, membrane protein, lipid transport |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus membrane; Multi-pass membrane protein: P20292 |
| Total number of polymer chains | 6 |
| Total formula weight | 113647.14 |
| Authors | Ferguson, A.D. (deposition date: 2007-06-07, release date: 2007-08-21, Last modification date: 2024-10-30) |
| Primary citation | Ferguson, A.D.,McKeever, B.M.,Xu, S.,Wisniewski, D.,Miller, D.K.,Yamin, T.T.,Spencer, R.H.,Chu, L.,Ujjainwalla, F.,Cunningham, B.R.,Evans, J.F.,Becker, J.W. Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Science, 317:510-512, 2007 Cited by PubMed Abstract: Leukotrienes are proinflammatory products of arachidonic acid oxidation by 5-lipoxygenase that have been shown to be involved in respiratory and cardiovascular diseases. The integral membrane protein FLAP is essential for leukotriene biosynthesis. We describe the x-ray crystal structures of human FLAP in complex with two leukotriene biosynthesis inhibitors at 4.0 and 4.2 angstrom resolution, respectively. The structures show that inhibitors bind in membrane-embedded pockets of FLAP, which suggests how these inhibitors prevent arachidonic acid from binding to FLAP and subsequently being transferred to 5-lipoxygenase, thereby preventing leukotriene biosynthesis. This structural information provides a platform for the development of therapeutics for respiratory and cardiovascular diseases. PubMed: 17600184DOI: 10.1126/science.1144346 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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