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. 2007 Jun 26;104(27):11239–11244. doi: 10.1073/pnas.0705055104

Fig. 3.

Fig. 3.

CMT residues that have potential tRNA interactions and the effect of CMT-causing mutations on tRNA aminoacylation. (A) Stereoview of the model of tRNA in a complex with GlyRS. Four of the nine resolved CMT-causing mutations are close to the tRNA interface: they are E71, P234′, I280, and G598. (B) Aminoacylation assay performed with the WT and seven mutant GlyRSs. Four different mutants of GlyRS (E71G, P234KY, D500N, and S581L) had WT-like activity, whereas three others (L129P, G240R, and G526R) were inactive.