3TDD
Crystal structure of yeast CP in complex with Belactosin C
Summary for 3TDD
| Entry DOI | 10.2210/pdb3tdd/pdb |
| Related | 1RYP 3E47 |
| Descriptor | Proteasome component Y7, Proteasome component C11, Proteasome component PRE2, ... (16 entities in total) |
| Functional Keywords | ubiquitin, inhibitor, proteasome, drug development, primed substrate binding channel, beta-sandwich flanked by alpha-helices, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Cytoplasm: P23639 P22141 P30656 P23724 P30657 P38624 P23638 P40303 P32379 P40302 P21242 P21243 P25043 P25451 |
| Total number of polymer chains | 28 |
| Total formula weight | 705473.70 |
| Authors | Korotkov, V.S.,Ludwig, A.,Larionov, O.V.,Lygin, A.V.,Groll, M.,de Meijere, A. (deposition date: 2011-08-10, release date: 2011-10-12, Last modification date: 2024-11-20) |
| Primary citation | Korotkov, V.S.,Ludwig, A.,Larionov, O.V.,Lygin, A.V.,Groll, M.,de Meijere, A. Synthesis and biological activity of optimized belactosin C congeners. Org.Biomol.Chem., 9:7791-7798, 2011 Cited by PubMed Abstract: Successful biochemical studies of the natural products belactosin A and C as well as their more stable acylated derivatives have proved them to be powerful proteasome inhibitors and thereby potential candidates as pharmacologically relevant active compounds. In order to understand their structure-biological activity relations in detail and to find ways of improving their biological activity, four new modified belactosin congeners have been synthesized and tested. One of them (compound 6) turned out to be a more potent inhibitor against HeLa cells than the known proteasome inhibitor MG132. PubMed: 21946808DOI: 10.1039/c1ob05661a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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