1fl0 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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
↑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
↑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
↑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
↑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
↑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
↑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
↑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
