Document Detail

Asymmetric structure and domain binding interfaces of human tyrosyl-tRNA synthetase studied by molecular dynamics simulations.
MedLine Citation:
PMID:  23334919     Owner:  NLM     Status:  In-Data-Review    
Human tyrosyl-tRNA synthetase (HsTyrRS) is composed of two structural modules: N-terminal catalytic core and an EMAP II-like C-terminal domain. The structures of these modules are known, but no crystal structure of the full-length HsTyrRS is currently available. An all-atom model of the full-length HsTyrRS was developed in this work. The structure, dynamics, and domain binding interfaces of HsTyrRS were investigated by extensive molecular dynamics (MD) simulations. Our data suggest that HsTyrRS in solution consists of a number of compact asymmetric conformations, which differ significantly by their rigidity, internal mobility, orientation of C-terminal modules, and the strength of interdomain binding. Interfaces of domain binding obtained in MD simulations are in perfect agreement with our previous coarse-grained hierarchical rotations technique simulations. Formation of the hydrogen bonds between R93 residue of the ELR cytokine motif and the residues A340 and E479 in the C-module was observed. This observation supports the idea that the lack of cytokine activity in the full-length HsTyrRS is explained by interactions between N-modules and C-modules, which block the ELR motif. Copyright © 2013 John Wiley & Sons, Ltd.
Oleksandr V Savytskyi; Semen O Yesylevskyy; Alexander I Kornelyuk
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular recognition : JMR     Volume:  26     ISSN:  1099-1352     ISO Abbreviation:  J. Mol. Recognit.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9004580     Medline TA:  J Mol Recognit     Country:  England    
Other Details:
Languages:  eng     Pagination:  113-20     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 John Wiley & Sons, Ltd.
Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Akademika Zabolotnogo Str., 150, Kyiv-03680, Ukraine.
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