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Structure of the ArgRS–GlnRS–AIMP1 complex and its implications for mammalian translation
  • Yaoyao Fu, Y. Kim, +12 authors Y. Cho
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences
  • 6 October 2014
Significance In higher eukaryotes, aminoacyl-tRNA synthetases (ARSs) are assembled to form a multisynthetase complex (MSC), which plays critical roles in translation and nontranslation functionsExpand
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Crystal structure of Thermoplasma acidophilum XerA recombinase shows large C‐shape clamp conformation and cis‐cleavage mode for nucleophilic tyrosine
Site‐specific Xer recombination plays a pivotal role in reshuffling genetic information. Here, we report the 2.5 Å crystal structure of XerA from the archaean Thermoplasma acidophilum.Expand
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The crystal structure of arginyl‐tRNA synthetase from Homo sapiens
Arginyl‐tRNA synthetase (ArgRS) is a tRNA‐binding protein that catalyzes the esterification of l‐arginine to its cognate tRNA. l‐Canavanine, a structural analog of l‐arginine, has recently beenExpand
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Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis
Survival of Clonorchis sinensis, a cause of human clonorchiasis, requires tegument proteins, which are localized to the tegumental outer surface membrane. These proteins play an important role in aExpand
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Crystal structure of Legionella pneumophila type IV secretion system effector LegAS4.
The SET domain of LegAS4, a type IV secretion system effector of Legionella pneumophila, is a eukaryotic protein motif involved in histone methylation and epigenetic modulation. The SET domain ofExpand
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Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state
DOCK (dedicator of cytokinesis) proteins are multidomain guanine nucleotide exchange factors (GEFs) for RHO GTPases that regulate intracellular actin dynamics. DOCK proteins share catalytic (DOCKExpand
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Crystal structure of RHOG and ELMO complex