Flexible 3D structure of Bos taurus tyrosyl-tRNA synthetase suggests the existence of the hinge mechanism provided by conservative Gly353 at interdomain linker
Mammalian tyrosyl-tRNA synthetase is composed of two structural modules: N-terminal catalytic miniTyrRS and non-catalytic cytokine-like C-terminal module connected by a flexible peptide linker. Till now, the 3D structure of any full-length mammalian TyrRS has not been solved by X-ray crystallography...
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| Published in: | Вiopolymers and Cell |
|---|---|
| Date: | 2012 |
| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Published: |
Інститут молекулярної біології і генетики НАН України
2012
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| Subjects: | |
| Online Access: | https://nasplib.isofts.kiev.ua/handle/123456789/156942 |
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| Journal Title: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Cite this: | Flexible 3D structure of Bos taurus tyrosyl-tRNA synthetase suggests the existence of the hinge mechanism provided by conservative Gly353 at interdomain linker / N.A. Pydiura, A.I. Kornelyuk // Вiopolymers and Cell. — 2012. — Т. 28, № 5. — С. 397-403. — Бібліогр.: 35 назв. — англ. |