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The structure of an AspRS–tRNA(Asp) complex reveals a tRNA-dependent control mechanism
The 2.6 Å resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs e...
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| Huvudupphovsmän: | , , , , , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Oxford University Press
2001
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC125622/ https://ncbi.nlm.nih.gov/pubmed/11566892 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/20.18.5290 |
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