Pub. Date : 1989 Nov 6
PMID : 2684669
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Our results show that EF-TuG20.GDP shares common features with the GTP-like conformation induced by kirromycin on wild-type EF-Tu. | Guanosine Diphosphate | Tu translation elongation factor, mitochondrial | Homo sapiens |
2 | Substitution of V20 by G in the consensus element G18HVDHGK24 of EF-Tu (referred to as EF-TuG20) strongly influences the interaction with GDP as well as the GTPase activity [Jacquet, E. & Parmeggiani, A. | Guanosine Diphosphate | Tu translation elongation factor, mitochondrial | Homo sapiens |
3 | Substitution of V20 by G in the consensus element G18HVDHGK24 of EF-Tu (referred to as EF-TuG20) strongly influences the interaction with GDP as well as the GTPase activity [Jacquet, E. & Parmeggiani, A. | Guanosine Diphosphate | Tu translation elongation factor, mitochondrial | Homo sapiens |
4 | Remarkably, EF-TuG20.GDP can support the enzymatic binding of aminoacyl-tRNA to ribosome.mRNA at low MgCl2 concentration, an effect that with wild-type EF-Tu can only occur in the presence of kirromycin. | Guanosine Diphosphate | Tu translation elongation factor, mitochondrial | Homo sapiens |
5 | Remarkably, EF-TuG20.GDP can support the enzymatic binding of aminoacyl-tRNA to ribosome.mRNA at low MgCl2 concentration, an effect that with wild-type EF-Tu can only occur in the presence of kirromycin. | Guanosine Diphosphate | Tu translation elongation factor, mitochondrial | Homo sapiens |
6 | Our results show that EF-TuG20.GDP shares common features with the GTP-like conformation induced by kirromycin on wild-type EF-Tu. | Guanosine Diphosphate | Tu translation elongation factor, mitochondrial | Homo sapiens |