Pub. Date : 2014 Nov 10
PMID : 25326326
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 2 | Correct codon-anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 3 | Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 4 | Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 5 | Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |
| 6 | Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis. | Guanosine Diphosphate | eukaryotic translation elongation factor 1 alpha 1 | Homo sapiens |