Journal
NATURE
Volume 461, Issue 7268, Pages 1234-1242Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature08403
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Funding
- Medical Research Council (UK)
- Wellcome Trust
- Louis-Jeantet Foundation
- Agouron Institute
- Human Frontiers Science Program and Emmanuel College, Cambridge
- Medical Research Council [MC_U105184332] Funding Source: researchfish
- MRC [MC_U105184332] Funding Source: UKRI
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The high-resolution structures of ribosomal subunits published in 2000 have revolutionized the field of protein translation. They facilitated the determination and interpretation of functional complexes of the ribosome by crystallography and electron microscopy. Knowledge of the precise positions of residues in the ribosome in various states has facilitated increasingly sophisticated biochemical and genetic experiments, as well as the use of new methods such as single-molecule kinetics. In this review, we discuss how the interaction between structural and functional studies over the last decade has led to a deeper understanding of the complex mechanisms underlying translation.
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