1ULH

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

Summary for 1ULH

• Entry DOI: 10.2210/pdb1ulh/pdb
• Descriptor: Tryptophanyl-tRNA synthetase (2 entities in total)
• Functional Keywords: aminoacylation, angiostatic cytokine, apoptosis, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P23381
• Total number of polymer chains: 2
• Total formula weight: 89583.87

Authors

Kise, Y.,Sengoku, T.,Ishii, R.,Yokoyama, S.,Park, S.G.,Lee, S.W.,Kim, S.,Nureki, O.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-09-12, release date: 2004-02-03, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.31 Å)