21058683

Source:http://linkedlifedata.com/resource/pubmed/id/21058683

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0002529, umls-concept:C0014653, umls-concept:C0019682, umls-concept:C0019699, umls-concept:C0030176, umls-concept:C0042760, umls-concept:C0086418, umls-concept:C0449432, umls-concept:C1179435, umls-concept:C1524073, umls-concept:C1548799, umls-concept:C1705248
pubmed:issue	49
pubmed:dateCreated	2010-12-14
pubmed:abstractText	Aminoacyl tRNA synthetases, components of the translation apparatus, have alternative functions outside of translation. The structural and mechanistic basis of these alternative functions is of great interest. As an example, reverse transcription of the HIV genome is primed by a human lysine-specific tRNA (tRNA(Lys3)) that is packaged (into the virion) by the HIV Gag protein with lysyl-tRNA synthetase (LysRS). Not understood is the structural basis for simultaneous packaging of tRNA(Lys3), LysRS, and Gag. Here, ab initio computational methods, together with our recent high-resolution 3-D structure of human LysRS, produced an energy-minimized model where Gag, tRNA(Lys), and LysRS form a ternary complex. Interestingly, the model requires normally homodimeric LysRS to dissociate into a monomer that bridges between Gag and tRNA(Lys3). Earlier experiments of others and new experiments presented here, which tested an engineered dissociated form of LysRS, were consistent with the ab initio "bridging monomer" model. The results support an emerging theme that alterative functions of tRNA synthetases may come, in part, from protein surfaces exposed by dynamic equilibria.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/CA92577, http://linkedlifedata.com/resource/pubmed/grant/GM 15539, http://linkedlifedata.com/resource/pubmed/grant/GM 23562, http://linkedlifedata.com/resource/pubmed/grant/R01 CA092577-08, http://linkedlifedata.com/resource/pubmed/grant/R01 CA092577-09, http://linkedlifedata.com/resource/pubmed/grant/R01 CA092577-10, http://linkedlifedata.com/resource/pubmed/grant/R01 GM015539-42, http://linkedlifedata.com/resource/pubmed/grant/R01 GM015539-43, http://linkedlifedata.com/resource/pubmed/grant/R01 GM015539-44, http://linkedlifedata.com/resource/pubmed/grant/R01 GM023562-34A1, http://linkedlifedata.com/resource/pubmed/grant/R01 GM023562-35, http://linkedlifedata.com/resource/pubmed/grant/R01 GM023562-36, http://linkedlifedata.com/resource/pubmed/grant/U54RR025204
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101157530
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Amino Acyl-tRNA Synthetases
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	1520-5207
pubmed:author	pubmed-author:MoeJ FJF, pubmed-author:MorrisGarrett MGM, pubmed-author:SchimmelPaulP, pubmed-author:ShapiroRyanR, pubmed-author:YangXiang-LeiXL
pubmed:issnType	Electronic
pubmed:day	16
pubmed:volume	114
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	16273-9
pubmed:dateRevised	2011-10-6
pubmed:meshHeading	pubmed-meshheading:21058683-Amino Acyl-tRNA Synthetases, pubmed-meshheading:21058683-HIV, pubmed-meshheading:21058683-Humans, pubmed-meshheading:21058683-Models, Molecular, pubmed-meshheading:21058683-Molecular Dynamics Simulation, pubmed-meshheading:21058683-Virus Assembly
pubmed:year	2010
pubmed:articleTitle	Packaging HIV virion components through dynamic equilibria of a human tRNA synthetase.
pubmed:affiliation	The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, California 92037, United States.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural