6QZP
High-resolution cryo-EM structure of the human 80S ribosome
This is a non-PDB format compatible entry.
Replaces: 6EK0Summary for 6QZP
| Entry DOI | 10.2210/pdb6qzp/pdb |
| EMDB information | 3883 |
| Descriptor | 28S rRNA (3773-MER), 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (86 entities in total) |
| Functional Keywords | human 80s ribosome, rrna, rrna modifications, high-resolution cryo-em, ribosome |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 81 |
| Total formula weight | 3254785.80 |
| Authors | Natchiar, S.K.,Myasnikov, A.G.,Kratzat, H.,Hazemann, I.,Klaholz, B.P. (deposition date: 2019-03-12, release date: 2019-04-24, Last modification date: 2024-04-24) |
| Primary citation | Natchiar, S.K.,Myasnikov, A.G.,Kratzat, H.,Hazemann, I.,Klaholz, B.P. Visualization of chemical modifications in the human 80S ribosome structure. Nature, 551:472-477, 2017 Cited by PubMed Abstract: Chemical modifications of human ribosomal RNA (rRNA) are introduced during biogenesis and have been implicated in the dysregulation of protein synthesis, as is found in cancer and other diseases. However, their role in this phenomenon is unknown. Here we visualize more than 130 individual rRNA modifications in the three-dimensional structure of the human ribosome, explaining their structural and functional roles. In addition to a small number of universally conserved sites, we identify many eukaryote- or human-specific modifications and unique sites that form an extended shell in comparison to bacterial ribosomes, and which stabilize the RNA. Several of the modifications are associated with the binding sites of three ribosome-targeting antibiotics, or are associated with degenerate states in cancer, such as keto alkylations on nucleotide bases reminiscent of specialized ribosomes. This high-resolution structure of the human 80S ribosome paves the way towards understanding the role of epigenetic rRNA modifications in human diseases and suggests new possibilities for designing selective inhibitors and therapeutic drugs. PubMed: 29143818DOI: 10.1038/nature24482 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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