5A0Q
Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core
Summary for 5A0Q
| Entry DOI | 10.2210/pdb5a0q/pdb |
| EMDB information | 2981 |
| Descriptor | PROTEASOME SUBUNIT ALPHA TYPE-6, PROTEASOME SUBUNIT BETA TYPE-3, PROTEASOME SUBUNIT BETA TYPE-2, ... (15 entities in total) |
| Functional Keywords | hydrolase, proteasome, 20s, adaahx3l3vs, ligand, inhibitor, drug design |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Cytoplasm : P60900 P49720 P49721 P28074 P20618 P28070 P25787 P25789 O14818 P28066 P25786 P25788 P28072 Q99436 |
| Total number of polymer chains | 28 |
| Total formula weight | 723185.21 |
| Authors | daFonseca, P.C.A.,Morris, E.P. (deposition date: 2015-04-22, release date: 2015-12-30, Last modification date: 2024-11-06) |
| Primary citation | Da Fonseca, P.C.A.,Morris, E.P. Cryo-Em Reveals the Conformation of a Substrate Analogue in the Human 20S Proteasome Core. Nat.Commun., 6:7573-, 2015 Cited by PubMed Abstract: The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, including key cellular regulators. Here we present the structure of the human 20S proteasome core bound to a substrate analogue inhibitor molecule, determined by electron cryo-microscopy (cryo-EM) and single-particle analysis at a resolution of around 3.5 Å. Our map allows the building of protein coordinates as well as defining the location and conformation of the inhibitor at the different active sites. These results open new prospects to tackle the proteasome functional mechanisms. Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general structural studies of protein-ligand interactions. PubMed: 26133119DOI: 10.1038/NCOMMS8573 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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