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1EUJ

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

Summary for 1EUJ
Entry DOI10.2210/pdb1euj/pdb
DescriptorENDOTHELIAL MONOCYTE ACTIVATING POLYPEPTIDE 2 (2 entities in total)
Functional Keywordsemap 2, emap ii, cytokine, trna synthetase, apoptosis, rna binding motif
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q12904
Total number of polymer chains2
Total formula weight36484.36
Authors
Kim, Y.,Shin, J.,Li, R.,Cheong, C.,Kim, S. (deposition date: 2000-04-17, release date: 2000-09-06, Last modification date: 2024-02-07)
Primary citationKim, Y.,Shin, J.,Li, R.,Cheong, C.,Kim, K.,Kim, S.
A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases.
J.Biol.Chem., 275:27062-27068, 2000
Cited by
PubMed Abstract: 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.
PubMed: 10852899
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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