期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 29, 期 5, 页码 250-256出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2004.03.002
关键词
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资金
- NCI NIH HHS [CA 92577] Funding Source: Medline
Human tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase (TrpRS) are closely related, dual function enzymes that act in protein biosynthesis and angiogenesis. The recent crystallographic structures of these two enzymes show that they adopt remarkably similar three-dimensional (3D) architectures, being more like each other than like their respective prokaryotic orthologs. In particular, adaptations to the anticodon recognition domain of TyrRS cause distinct appended domains in TyrRS and TrpRS to occupy the same 3D space and thus to mask a common surface on each synthetase. Thought to be important for cell-signaling activity, this surface is made accessible by proteolytic cleavage, thereby activating the cell-signaling function of these enzymes.
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