4AZN
Murine epidermal fatty acid-binding protein (FABP5), apo form, poly- his tag-mediated crystal packing
Summary for 4AZN
| Entry DOI | 10.2210/pdb4azn/pdb |
| Related | 4AZM 4AZO 4AZP 4AZQ 4AZR |
| Descriptor | FATTY ACID-BINDING PROTEIN, EPIDERMAL (2 entities in total) |
| Functional Keywords | lipid binding protein, lipid carrier protein, endocannabinoid, beta-barrel, beta-clamshell, domain swapping |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) |
| Total number of polymer chains | 2 |
| Total formula weight | 34687.65 |
| Authors | Sanson, B.,Wang, T.,Sun, J.,Kaczocha, M.,Ojima, I.,Deutsch, D.,Li, H. (deposition date: 2012-06-26, release date: 2013-08-07, Last modification date: 2023-12-20) |
| Primary citation | Sanson, B.,Wang, T.,Sun, J.,Wang, L.,Kaczocha, M.,Ojima, I.,Deutsch, D.,Li, H. Crystallographic Study of Fabp5 as an Intracellular Endocannabinoid Transporter. Acta Crystallogr.,Sect.D, 70:290-, 2014 Cited by PubMed Abstract: In addition to binding intracellular fatty acids, fatty-acid-binding proteins (FABPs) have recently been reported to also transport the endocannabinoids anandamide (AEA) and 2-arachidonoylglycerol (2-AG), arachidonic acid derivatives that function as neurotransmitters and mediate a diverse set of physiological and psychological processes. To understand how the endocannabinoids bind to FABPs, the crystal structures of FABP5 in complex with AEA, 2-AG and the inhibitor BMS-309403 were determined. These ligands are shown to interact primarily with the substrate-binding pocket via hydrophobic interactions as well as a common hydrogen bond to the Tyr131 residue. This work advances our understanding of FABP5-endocannabinoid interactions and may be useful for future efforts in the development of small-molecule inhibitors to raise endocannabinoid levels. PubMed: 24531463DOI: 10.1107/S1399004713026795 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
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