2004年2月
A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase
NATURE STRUCTURAL & MOLECULAR BIOLOGY
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- 巻
- 11
- 号
- 2
- 開始ページ
- 149
- 終了ページ
- 156
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/nsmb722
- 出版者・発行元
- NATURE PUBLISHING GROUP
Human tryptophanyl-tRNA synthetase (TrpRS) is secreted into the extracellular region of vascular endothelial cells. The splice variant form (mini TrpRS) functions in vascular endothelial cell apoptosis as an angiostatic cytokine. In contrast, the closely related human tyrosyl-tRNA synthetase (TyrRS) functions as an angiogenic cytokine in its truncated form (mini TyrRS). Here, we determined the crystal structure of human mini TrpRS at a resolution of 2.3 Angstrom and compared the structure with those of prokaryotic TrpRS and human mini TyrRS. Deletion of the tRNA anticodon-binding (TAB) domain insertion, consisting of eight residues in the human TrpRS, abolished the enzyme's apoptotic activity for endothelial cells, whereas its translational catalysis and cell-binding activities remained unchanged. Thus, we have identified the inserted peptide motif that activates the angiostatic signaling.
- リンク情報
- ID情報
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- DOI : 10.1038/nsmb722
- ISSN : 1545-9985
- Web of Science ID : WOS:000220281000012