Binding and enantiomeric selectivity of threonyl-tRNA synthetase

Malde, Alpeshkumar K. and Mark, Alan E. (2009) Binding and enantiomeric selectivity of threonyl-tRNA synthetase. Journal of the American Chemical Society, 131 11: 3848-3849. doi:10.1021/ja9002124


Author Malde, Alpeshkumar K.
Mark, Alan E.
Title Binding and enantiomeric selectivity of threonyl-tRNA synthetase
Journal name Journal of the American Chemical Society   Check publisher's open access policy
ISSN 0002-7863
Publication date 2009-02-27
Year available 2009
Sub-type Article (original research)
DOI 10.1021/ja9002124
Open Access Status Not yet assessed
Volume 131
Issue 11
Start page 3848
End page 3849
Total pages 2
Editor Peter J Stang
Place of publication United States
Publisher American Chemical Society
Language eng
Subject C1
030402 Biomolecular Modelling and Design
970103 Expanding Knowledge in the Chemical Sciences
Abstract A combination of MD simulations and free energy calculations have been used to propose a new model for the binding of amino acids to threonyl-tRNA-synthetase which not only yields a stable binding mode for L-Ser but also can explain the mechanism by which the editing domains of aminoacyl-tRNA-synthetases are enantiomeric selective preferentially binding D-amino acids.
Keyword Protein-Synthesis
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID m72
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
School of Chemistry and Molecular Biosciences
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 10 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 10 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Thu, 03 Sep 2009, 18:20:39 EST by Mr Andrew Martlew on behalf of School of Chemistry & Molecular Biosciences