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Article

Large Conformational Changes of Insertion 3 in Human Glycyl-tRNA Synthetase (hGlyRS) during Catalysis.

The Journal of biological chemistry - 11 Mar 2016

Deng Xiangyu, Qin Xiangjing, Chen Lei, Jia Qian, Zhang Yonghui, Zhang Zhiyong, Lei Dongsheng, Ren Gang, Zhou Zhihong, Wang Zhong, Li Qing, Xie Wei

Abstract excerpt

Glycyl-tRNA synthetase (GlyRS) is the enzyme that covalently links glycine to cognate tRNA for translation. It is of great research interest because of its nonconserved quaternary structures, unique species-specific aminoacylation properties, and noncanonical functions in neurological diseases, but none of these is fully understood. We report two crystal structures of human GlyRS variants, in the free form and in...

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Identifiers

PMID: 26797133
DOI: 10.1074/jbc.M115.679126
PMCID: PMC4786711

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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