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Structure of the human 80S ribosome
Author(s) -
Heena Khatter,
Alexander G. Myasnikov,
S. Kundhavai Natchiar,
Bruno P. Klaholz
Publication year - 2015
Publication title -
nature
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 15.993
H-Index - 1226
eISSN - 1476-4687
pISSN - 0028-0836
DOI - 10.1038/nature14427
Subject(s) - ribosome , eukaryotic ribosome , transfer rna , ribosomal rna , ribosomal protein , rna , translation (biology) , biophysics , protein biosynthesis , structural biology , computational biology , 5.8s ribosomal rna , a site , protein subunit , chemistry , biology , microbiology and biotechnology , biochemistry , binding site , messenger rna , gene
Ribosomes are translational machineries that catalyse protein synthesis. Ribosome structures from various species are known at the atomic level, but obtaining the structure of the human ribosome has remained a challenge; efforts to address this would be highly relevant with regard to human diseases. Here we report the near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building. The structure has an average resolution of 3.6 Å, reaching 2.9 Å resolution in the most stable regions. It provides unprecedented insights into ribosomal RNA entities and amino acid side chains, notably of the transfer RNA binding sites and specific molecular interactions with the exit site tRNA. It reveals atomic details of the subunit interface, which is seen to remodel strongly upon rotational movements of the ribosomal subunits. Furthermore, the structure paves the way for analysing antibiotic side effects and diseases associated with deregulated protein synthesis.

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