ArticleStructure (London, England : 1993)2007
Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase.
Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
- Neuropilin 1 and its inhibitory ligand mini-tryptophanyl-tRNA synthetase inversely regulate VE-cadherin turnover and vascular permeability.Nature communications · 2022Article
- The zinc-binding domain of mammalian prolyl-tRNA synthetase is indispensable for catalytic activity and organism viability.iScience · 2021Article
- Unique roles of tryptophanyl-tRNA synthetase in immune control and its therapeutic implications.Experimental & molecular medicine · 2019Review
- Tryptophanyl-tRNA synthetase mediates high-affinity tryptophan uptake into human cells.The Journal of biological chemistry · 2018Article
- An alternative conformation of human TrpRS suggests a role of zinc in activating non-enzymatic function.RNA biology · 2018Article
- Thrombopoietic stimulating activity of rhTyrRS (Y341A).Scientific reports · 2017Article
- Coding of Class I and II Aminoacyl-tRNA Synthetases.Advances in experimental medicine and biology · 2017Review
- Identification of a residue crucial for the angiostatic activity of human mini tryptophanyl-tRNA synthetase by focusing on its molecular evolution.Scientific reports · 2016Article
- Selective Inhibition of Bacterial Tryptophanyl-tRNA Synthetases by Indolmycin Is Mechanism-based.The Journal of biological chemistry · 2016Article
- Expression, purification, and characterization of rhTyrRS.BMC biotechnology · 2014Article
- Architecture and metamorphosis.Topics in current chemistry · 2014Review
- Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design.Molecular and biochemical parasitology · 2013Article
- Capture and quality control mechanisms for adenosine-5'-triphosphate binding.Journal of the American Chemical Society · 2013Article
- Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-γ and p53 signaling.Nature chemical biology · 2012Article
- Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Crystal structures of three protozoan homologs of tryptophanyl-tRNA synthetase.Molecular and biochemical parasitology · 2011Article
- Structure of Leishmania major methionyl-tRNA synthetase in complex with intermediate products methionyladenylate and pyrophosphate.Biochimie · 2011Article
- The structure of tryptophanyl-tRNA synthetase from Giardia lamblia reveals divergence from eukaryotic homologs.Journal of structural biology · 2010Article
- Crystal structures of Saccharomyces cerevisiae tryptophanyl-tRNA synthetase: new insights into the mechanism of tryptophan activation and implications for anti-fungal drug design.Nucleic acids research · 2010Article
- Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Higher eukaryote tRNA synthetases have expanded functions that come from enlarged, more differentiated structures that were adapted to fit aminoacylation function. How those adaptations affect catalytic mechanisms is not known. Presented here is the structure of a catalytically active natural splice variant of human tryptophanyl-tRNA synthetase (TrpRS) that is a potent angiostatic factor. This and related structures suggest that a eukaryote-specific N-terminal extension of the core enzyme changed substrate recognition by forming an active site cap. At the junction of the extension and core catalytic unit, an arginine is recruited to replace a missing landmark lysine almost 200 residues away. Mutagenesis, rapid kinetic, and substrate binding studies support the functional significance of the cap and arginine recruitment. Thus, the enzyme function of human TrpRS has switched more to the N terminus of the sequence. This switch has the effect of creating selective pressure to retain the N-terminal extension for functional expansion.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.