The inhibition mechanism of human 20S proteasomes enables next-generation inhibitor design

Science

Volumn 353, Issue 6299, 2016, Pages 594-598

  Schrader, Jil ^a   Henneberg, Fabian ^a   Mata, Ricardo A ^b   Tittmann, Kai ^b   Schneider, Thomas R ^c   Stark, Holger ^a   Bourenkov, Gleb ^c   Chari, Ashwin ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

^c DESY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

20S PROTEASOME; DIHYDROEPONEMYCIN; EPOXOMICIN; NATURAL PRODUCT; OPROZOMIB; PROTEASOME; PROTEASOME INHIBITOR; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; BORON DERIVATIVE; BORONIC ACID DERIVATIVE; BORTEZOMIB; DELANZOMIB; GLYCINE; IXAZOMIB; THREONINE;

CANCER; CATALYST; COMPLEXITY; CRYSTAL STRUCTURE; DESIGN; DRUG; HEMATOLOGY; HYDROLYSIS; INHIBITION; PEPTIDE; PROTEOMICS; TUMOR;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; CYCLIZATION; DRUG DESIGN; DRUG PROTEIN BINDING; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; FEMALE; HELA CELL LINE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; ANALOGS AND DERIVATIVES; BIOCATALYSIS; CHEMISTRY; DRUG EFFECTS; PROTEIN CONFORMATION; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

ANTINEOPLASTIC AGENTS; BIOCATALYSIS; BORON COMPOUNDS; BORONIC ACIDS; BORTEZOMIB; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; GLYCINE; HUMANS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEASOME INHIBITORS; PROTEIN CONFORMATION; THREONINE;

EID: 84982830486     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaf8993     Document Type: Article

References (19)

1. M. Bochtler, L. Ditzel, M. Groll, C. Hartmann, R. Huber, Annu. Rev. Biophys. Biomol. Struct. 28, 295-317 (1999).
2. E. Kish-Trier, C. P. Hill, Annu Rev Biophys 42, 29-49 (2013).
3. A. Ciechanover, Cell 79, 13-21 (1994).
4. D. Finley, Annu. Rev. Biochem. 78, 477-513 (2009).
5. M. Groll et al., Nature 386, 463-471 (1997).
6. W. Harshbarger, C. Miller, C. Diedrich, J. Sacchettini, Structure 23, 418-424 (2015).
7. P. C. da Fonseca, E. P. Morris, Nat. Commun. 6, 7573 (2015).
8. A. Chari et al., Nat. Methods 12, 859-865 (2015).
9. E. M. Huber et al., Cell 148, 727-738 (2012).
10. E. M. Huber et al., Nat. Commun. 7, 10900 (2016).
11. E. M. Huber, W. Heinemeyer, M. Groll, Structure 23, 407-417 (2015).
12. S. D. Demo et al., Cancer Res. 67, 6383-6391 (2007).
13. T. A. Grigoreva, V. G. Tribulovich, A. V. Garabadzhiu, G. Melino, N. A. Barlev, Oncotarget 6, 24733-24749 (2015).
14. M. Groll, K. B. Kim, N. Kairies, R. Huber, C. M. Crews, J. Am. Chem. Soc. 122, 1237-1238 (2000).
15. J. F. Lynas, P. Harriott, A. Healy, M. A. McKervey, B. Walker, Bioorg. Med. Chem. Lett. 8, 373-378 (1998).
16. M. A. Gräwert et al., Angew. Chem. Int. Ed. Engl. 50, 542-544 (2011).
17. R. C. Kane, A. T. Farrell, R. Sridhara, R. Pazdur, Clin. Cancer Res. 12, 2955-2960 (2006).
18. M. Shirley, Drugs 76, 405-411 (2016).
19. M. K. Bennett, C. J. Kirk, Curr. Opin. Drug Discov. Devel. 11, 616-625 (2008).