2MGY
Solution structure of the mitochondrial translocator protein (TSPO) in complex with its high-affinity ligand PK11195
Summary for 2MGY
| Entry DOI | 10.2210/pdb2mgy/pdb |
| NMR Information | BMRB: 19608 |
| Descriptor | Translocator protein, N-[(2R)-butan-2-yl]-1-(2-chlorophenyl)-N-methylisoquinoline-3-carboxamide (2 entities in total) |
| Functional Keywords | membrane protein, translocator protein (tspo), protein-ligand complex, mitochondrial membrane, pk11195, dpc micelles, peripheral benzodiazepine receptor, helical membrane channel protein |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 19151.54 |
| Authors | Jaremko, M.,Jaremko, L.,Giller, K.,Becker, S.,Zweckstetter, M. (deposition date: 2013-11-11, release date: 2014-04-02, Last modification date: 2024-05-15) |
| Primary citation | Jaremko, L.,Jaremko, M.,Giller, K.,Becker, S.,Zweckstetter, M. Structure of the mitochondrial translocator protein in complex with a diagnostic ligand. Science, 343:1363-1366, 2014 Cited by PubMed Abstract: The 18-kilodalton translocator protein TSPO is found in mitochondrial membranes and mediates the import of cholesterol and porphyrins into mitochondria. In line with the role of TSPO in mitochondrial function, TSPO ligands are used for a variety of diagnostic and therapeutic applications in animals and humans. We present the three-dimensional high-resolution structure of mammalian TSPO reconstituted in detergent micelles in complex with its high-affinity ligand PK11195. The TSPO-PK11195 structure is described by a tight bundle of five transmembrane α helices that form a hydrophobic pocket accepting PK11195. Ligand-induced stabilization of the structure of TSPO suggests a molecular mechanism for the stimulation of cholesterol transport into mitochondria. PubMed: 24653034DOI: 10.1126/science.1248725 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
