Model of the structure of the eukaryotic ribosomal translation termination complex

التفاصيل البيبلوغرافية
العنوان: Model of the structure of the eukaryotic ribosomal translation termination complex
المؤلفون: Lev L. Kisselev, Yu. N. Vorobjev
المصدر: Molecular Biology. 41:93-101
بيانات النشر: Pleiades Publishing Ltd, 2007.
سنة النشر: 2007
مصطلحات موضوعية: Genetics, A-site, Eukaryotic translation, Five prime untranslated region, Structural Biology, Stereochemistry, Transfer RNA, Biophysics, Biology, Release factor, Eukaryotic Ribosome, Stop codon, Ribosomal binding site
الوصف: Models of the atomic structure of the eukaryotic translation termination complex containing mRNA, P-site tRNAPhe, human class 1 release factor eRF1, and 80S ribosome, were constructed by computational modeling. The modeling was based on the assumed structural-functional similarity between the tRNA and eFR1 molecules in the ribosomal A site. The known atomic structure of the 70S ribosome complexed with mRNA as well as the P-and A-site tRNAsPhe was used as a structural template for the modeling. The eRF1 molecule bound in the A site undergoes substantial conformational changes so that the mutual configuration of the N and M domains matches the overall tRNA shape. Two models of eRF1 binding to mRNA at the A site in the presence of P-site tRNAPhe were generated. A characteristic of these models is complementary interactions between the mRNA stop codon and the grooves at different sides of the surface of the eRF1 fragment, containing helix α2, NIKS loop, and helix α3 of the N domain. In model 1, the nucleotides of the mRNA stop codon at the A site are approximately equidistant (∼15 A) from the N (motifs NIKS and YxCxxxF) and C domains. In model 2, the stop codon is close to the N-domain motifs NIKS and YxCxxxF. Both models fit genetic and biochemical experimental data. The choice of a particular model requires additional studies.
تدمد: 1608-3245
0026-8933
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::00a5f754af97b74dec61e05d820987b0
https://doi.org/10.1134/s002689330701013x
حقوق: CLOSED
رقم الأكسشن: edsair.doi...........00a5f754af97b74dec61e05d820987b0
قاعدة البيانات: OpenAIRE