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| - | [[Image:1n3l.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1n3l| PDB=1n3l | SCENE= }} | | {{STRUCTURE_1n3l| PDB=1n3l | SCENE= }} |
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| - | '''Crystal structure of a human aminoacyl-tRNA synthetase cytokine'''
| + | ===Crystal structure of a human aminoacyl-tRNA synthetase cytokine=== |
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| - | ==Overview==
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| - | The 20 aminoacyl-tRNA synthetases catalyze the first step of protein synthesis and establish the rules of the genetic code through aminoacylation reactions. Biological fragments of two human enzymes, tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase, connect protein synthesis to cell-signaling pathways including angiogenesis. Alternative splicing or proteolysis produces these fragments. The proangiogenic N-terminal fragment mini-TyrRS has IL-8-like cytokine activity that, like other CXC cytokines, depends on a Glu-Leu-Arg motif. Point mutations in this motif abolish cytokine activity. The full-length native TyrRS lacks cytokine activity. No structure has been available for any mammalian tRNA synthetase that, in turn, might give insight into why mini-TyrRS and not TyrRS has cytokine activities. Here, the structure of human mini-TyrRS, which contains both the catalytic and the anticodon recognition domain, is reported to a resolution of 1.18 A. The critical Glu-Leu-Arg motif is located on an internal alpha-helix of the catalytic domain, where the guanidino side chain of R is part of a hydrogen-bonding network tethering the anticodon-recognition domain back to the catalytic site. Whereas the catalytic domains of the human and bacterial enzymes superimpose, the spatial disposition of the anticodon recognition domain relative to the catalytic domain is unique in mini-TyrRS relative to the bacterial orthologs. This unique orientation of the anticodon-recognition domain can explain why the fragment mini-TyrRS, and not full-length native TyrRS, is active in cytokine-signaling pathways.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12427973}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12427973 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12427973}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rossmann fold as catalytic domain]] | | [[Category: Rossmann fold as catalytic domain]] |
| | [[Category: Unique anticodon recognition domain]] | | [[Category: Unique anticodon recognition domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:02:49 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:36:24 2008'' |
Revision as of 01:36, 28 July 2008
Template:STRUCTURE 1n3l
Crystal structure of a human aminoacyl-tRNA synthetase cytokine
Template:ABSTRACT PUBMED 12427973
About this Structure
1N3L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a human aminoacyl-tRNA synthetase cytokine., Yang XL, Skene RJ, McRee DE, Schimmel P, Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15369-74. Epub 2002 Nov 11. PMID:12427973
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