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<StructureSection load='1euj' size='340' side='right'caption='[[1euj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1euj' size='340' side='right'caption='[[1euj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1euj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EUJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1euj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUJ FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1euj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1euj RCSB], [http://www.ebi.ac.uk/pdbsum/1euj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1euj ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1euj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euj OCA], [https://pdbe.org/1euj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1euj RCSB], [https://www.ebi.ac.uk/pdbsum/1euj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1euj ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:[http://omim.org/entry/260600 260600]]. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.<ref>PMID:21092922</ref>
[https://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN] Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:[https://omim.org/entry/260600 260600]. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.<ref>PMID:21092922</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.<ref>PMID:10358004</ref> <ref>PMID:11306575</ref> <ref>PMID:12237313</ref> <ref>PMID:11818442</ref> <ref>PMID:19362550</ref> <ref>PMID:11157763</ref>
[https://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN] Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.<ref>PMID:10358004</ref> <ref>PMID:11306575</ref> <ref>PMID:12237313</ref> <ref>PMID:11818442</ref> <ref>PMID:19362550</ref> <ref>PMID:11157763</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1euj ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1euj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:10852899</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1euj" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cheong, C]]
[[Category: Cheong C]]
[[Category: Kim, S]]
[[Category: Kim S]]
[[Category: Kim, Y]]
[[Category: Kim Y]]
[[Category: Li, R]]
[[Category: Li R]]
[[Category: Shin, J]]
[[Category: Shin J]]
[[Category: Apoptosis]]
[[Category: Cytokine]]
[[Category: Emap 2]]
[[Category: Emap ii]]
[[Category: Rna binding motif]]
[[Category: Trna synthetase]]

Latest revision as of 10:07, 7 February 2024

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

Structural highlights

1euj is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

AIMP1_HUMAN Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:260600. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.[1]

Function

AIMP1_HUMAN Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.[2] [3] [4] [5] [6] [7]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Feinstein M, Markus B, Noyman I, Shalev H, Flusser H, Shelef I, Liani-Leibson K, Shorer Z, Cohen I, Khateeb S, Sivan S, Birk OS. Pelizaeus-Merzbacher-like disease caused by AIMP1/p43 homozygous mutation. Am J Hum Genet. 2010 Dec 10;87(6):820-8. doi: 10.1016/j.ajhg.2010.10.016. Epub, 2010 Nov 18. PMID:21092922 doi:10.1016/j.ajhg.2010.10.016
  2. ↑ Park SG, Jung KH, Lee JS, Jo YJ, Motegi H, Kim S, Shiba K. Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. J Biol Chem. 1999 Jun 11;274(24):16673-6. PMID:10358004
  3. ↑ Shalak V, Kaminska M, Mitnacht-Kraus R, Vandenabeele P, Clauss M, Mirande M. The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component. J Biol Chem. 2001 Jun 29;276(26):23769-76. Epub 2001 Apr 16. PMID:11306575 doi:10.1074/jbc.M100489200
  4. ↑ Park SG, Kang YS, Ahn YH, Lee SH, Kim KR, Kim KW, Koh GY, Ko YG, Kim S. Dose-dependent biphasic activity of tRNA synthetase-associating factor, p43, in angiogenesis. J Biol Chem. 2002 Nov 22;277(47):45243-8. Epub 2002 Sep 16. PMID:12237313 doi:10.1074/jbc.M207934200
  5. ↑ Park H, Park SG, Lee JW, Kim T, Kim G, Ko YG, Kim S. Monocyte cell adhesion induced by a human aminoacyl-tRNA synthetase-associated factor, p43: identification of the related adhesion molecules and signal pathways. J Leukoc Biol. 2002 Feb;71(2):223-30. PMID:11818442
  6. ↑ Tandle AT, Calvani M, Uranchimeg B, Zahavi D, Melillo G, Libutti SK. Endothelial monocyte activating polypeptide-II modulates endothelial cell responses by degrading hypoxia-inducible factor-1alpha through interaction with PSMA7, a component of the proteasome. Exp Cell Res. 2009 Jul 1;315(11):1850-9. doi: 10.1016/j.yexcr.2009.03.021. Epub, 2009 Apr 10. PMID:19362550 doi:10.1016/j.yexcr.2009.03.021
  7. ↑ Renault L, Kerjan P, Pasqualato S, Menetrey J, Robinson JC, Kawaguchi S, Vassylyev DG, Yokoyama S, Mirande M, Cherfils J. Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry. EMBO J. 2001 Feb 1;20(3):570-8. PMID:11157763 doi:10.1093/emboj/20.3.570

1euj, resolution 1.80Å

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