4.6 Review Book Chapter

Structural Basis of the Translational Elongation Cycle

期刊

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 82
卷 82, 期 -, 页码 203-236

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ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-113009-092313

关键词

translation; ribosome; protein synthesis; decoding; translocation; peptidyl transfer

资金

  1. Medical Research Council (UK) [U105184332]
  2. Wellcome Trust
  3. Agouron Institute
  4. Louis-Jeantet Foundation
  5. Peterhouse, Cambridge
  6. Medical Research Council [MC_U105184332] Funding Source: researchfish
  7. MRC [MC_U105184332] Funding Source: UKRI

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The sequential addition of amino acids to a growing polypeptide chain is carried out by the ribosome in a complicated multistep process called the elongation cycle. It involves accurate selection of each aminoacyl tRNA as dictated by the mRNA codon, catalysis of peptide bond formation, and movement of the tRNAs and mRNA through the ribosome. The process requires the GTPase factors elongation factor Tu (EF-Tu) and EF-G. Not surprisingly, large conformational changes in both the ribosome and its tRNA substrates occur throughout protein elongation. Major advances in our understanding of the elongation cycle have been made in the past few years as a result of high-resolution crystal structures that capture various states of the process, as well as biochemical and computational studies.

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