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The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue
Leucyl-, isoleucyl- and valyl-tRNA synthetases are closely related large monomeric class I synthetases. Each contains a homologous insertion domain of ∼200 residues, which is thought to permit them to hydrolyse (‘edit’) cognate tRNA that has been mischarged with a chemically similar but non-cognate...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Oxford University Press
2000
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC384370/ https://ncbi.nlm.nih.gov/pubmed/10811626 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/19.10.2351 |
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