1euj

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1euj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euj OCA], [http://www.ebi.ac.uk/pdbsum/1euj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1euj RCSB]</span>
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[[Category: trna synthetase]]
[[Category: trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:09:52 2008''

Revision as of 17:09, 30 March 2008

Image:1euj.gif


PDB ID 1euj

Drag the structure with the mouse to rotate
, resolution 1.8Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



A NOVEL ANTI-TUMOR CYTOKINE CONTAINS A RNA-BINDING MOTIF PRESENT IN AMINOACYL-TRNA SYNTHETASES


Overview

Endothelial monocyte-activating polypeptide II (EMAP II) is a novel pro-apoptotic cytokine that shares sequence homology with the C-terminal regions of several tRNA synthetases. Pro-EMAP II, the precursor of EMAP II, is associated with the multi-tRNA synthetase complex and facilitates aminoacylation activity. The structure of human EMAP II, solved at 1.8 A resolution, revealed the oligomer-binding fold for binding different tRNAs and a domain that is structurally homologous to other chemokines. The similar structures to the RNA binding motif of EMAP II was previously observed in the anticodon binding domain of yeast Asp-tRNA synthetase (AspRSSC) and the B2 domain of Thermus thermophilus Phe-tRNA synthetase. The RNA binding pattern of EMAP II is likely to be nonspecific, in contrast to the AspRSSC. The peptide sequence that is responsible for cytokine activity is located, for the most part, in the beta1 strand. It is divided into two regions by a neighboring loop.

About this Structure

1EUJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases., Kim Y, Shin J, Li R, Cheong C, Kim K, Kim S, J Biol Chem. 2000 Sep 1;275(35):27062-8. PMID:10852899

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