4ZYO
Crystal Structure of Human Integral Membrane Stearoyl-CoA Desaturase with Substrate
Summary for 4ZYO
| Entry DOI | 10.2210/pdb4zyo/pdb |
| Descriptor | Acyl-CoA desaturase, ZINC ION, STEAROYL-COENZYME A, ... (5 entities in total) |
| Functional Keywords | membrane protein, desaturase, metal binding protein, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Endoplasmic reticulum membrane ; Multi-pass membrane protein : O00767 |
| Total number of polymer chains | 1 |
| Total formula weight | 38473.64 |
| Authors | Wang, H.,Klein, M.G.,Lane, W.,Snell, G.,Levin, I.,Li, K.,Zou, H.,Sang, B.-C. (deposition date: 2015-05-21, release date: 2015-06-17, Last modification date: 2024-03-06) |
| Primary citation | Wang, H.,Klein, M.G.,Zou, H.,Lane, W.,Snell, G.,Levin, I.,Li, K.,Sang, B.C. Crystal structure of human stearoyl-coenzyme A desaturase in complex with substrate. Nat.Struct.Mol.Biol., 22:581-585, 2015 Cited by PubMed Abstract: Stearoyl-coenzyme A desaturase-1 (SCD1) has an important role in lipid metabolism, and SCD1 inhibitors are potential therapeutic agents for the treatment of metabolic diseases and cancers. Here we report the 3.25-Å crystal structure of human SCD1 in complex with its substrate, stearoyl-coenzyme A, which defines the new SCD1 dimetal catalytic center and reveals the determinants of substrate binding to provide insights into the catalytic mechanism of desaturation of the stearoyl moiety. The structure also provides a mechanism for localization of SCD1 in the endoplasmic reticulum: human SCD1 folds around a tight hydrophobic core formed from four long α-helices that presumably function as an anchor spanning the endoplasmic reticulum membrane. Furthermore, our results provide a framework for the rational design of pharmacological inhibitors targeting the SCD1 enzyme. PubMed: 26098317DOI: 10.1038/nsmb.3049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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