Title : tRNA-ribosome interactions.

Pub. Date : 1995 Nov-Dec

PMID : 8722020






4 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
2 Elongation factor Tu (EF-Tu) undergoes a dramatic structural transition from its GDP-bound form to its active GTP-bound form, in which it binds aa-tRNA (aminoacyl-tRNA) in ternary complex. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
3 The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens
4 The effects of substitution mutations at three sites in domain I of EF-Tu, Gln124, Leu120, and Tyr160, all of which point into the domain I-domain III interface in both the GTP and GDP conformations of EF-Tu, were examined. Guanosine Diphosphate eukaryotic translation elongation factor 1 alpha 1 Homo sapiens