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-Structure paper
Title | CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Year 2019 |
Publish date | Jun 16, 2017 (structure data deposition date) |
Authors | Blocquel, D. / Sun, L. / Matuszek, Z. / Li, S. / Weber, T. / Kuhle, B. / Kooi, G. / Wei, N. / Baets, J. / Pan, T. ...Blocquel, D. / Sun, L. / Matuszek, Z. / Li, S. / Weber, T. / Kuhle, B. / Kooi, G. / Wei, N. / Baets, J. / Pan, T. / Schimmel, P. / Yang, X.L. |
External links | Proc. Natl. Acad. Sci. USA / PubMed:31501329 |
Methods | X-ray diffraction |
Resolution | 2.787 - 3.696 Å |
Structure data | PDB-5w6m: PDB-6o76: |
Chemicals | ChemComp-CL: ChemComp-HOH: |
Source |
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Keywords | LIGASE / tRNA-synthetase / CMT mutant / tRNA / CMT / WHEP domain / alpha beta domain |