1ULH

A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase

1ULH の概要

• エントリーDOI: 10.2210/pdb1ulh/pdb
• 分子名称: Tryptophanyl-tRNA synthetase (2 entities in total)
• 機能のキーワード: aminoacylation, angiostatic cytokine, apoptosis, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P23381
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89583.87

構造登録者

Kise, Y.,Sengoku, T.,Ishii, R.,Yokoyama, S.,Park, S.G.,Lee, S.W.,Kim, S.,Nureki, O.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-09-12, 公開日: 2004-02-03, 最終更新日: 2023-12-27)

主引用文献

Kise, Y.,Lee, S.W.,Park, S.G.,Fukai, S.,Sengoku, T.,Ishii, R.,Yokoyama, S.,Kim, S.,Nureki, O.
A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase
Nat.Struct.Mol.Biol., 11:149-156, 2004

PubMed Abstract: 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 A 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.

PubMed: 14730354
DOI: 10.1038/nsmb722

実験手法

X-RAY DIFFRACTION (2.31 Å)