4ga0

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{{STRUCTURE_4ga0| PDB=4ga0 | SCENE= }}
 
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===Structure of the N-terminal domain of Nup358===
 
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{{ABSTRACT_PUBMED_22959972}}
 
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==Disease==
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==Structure of the N-terminal domain of Nup358==
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[[http://www.uniprot.org/uniprot/RBP2_HUMAN RBP2_HUMAN]] Defects in RANBP2 are the cause of encephalopathy acute infection-induced type 3 (IIAE3) [MIM:[http://omim.org/entry/608033 608033]]. A rapidly progressive encephalopathy manifesting in susceptibile individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem. Note=Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (PubMed:19118815).<ref>PMID:19118815</ref>
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<StructureSection load='4ga0' size='340' side='right'caption='[[4ga0]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[4ga0]] is a 1 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=4GA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GA0 FirstGlance]. <br>
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[[http://www.uniprot.org/uniprot/RBP2_HUMAN RBP2_HUMAN]] E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Could also have isomerase or chaperone activity and may bind RNA or DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1.<ref>PMID:11792325</ref><ref>PMID:12032081</ref><ref>PMID:15378033</ref><ref>PMID:15931224</ref>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ga0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ga0 OCA], [https://pdbe.org/4ga0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ga0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ga0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ga0 ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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[[4ga0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GA0 OCA].
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== Disease ==
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[https://www.uniprot.org/uniprot/RBP2_HUMAN RBP2_HUMAN] Defects in RANBP2 are the cause of encephalopathy acute infection-induced type 3 (IIAE3) [MIM:[https://omim.org/entry/608033 608033]. A rapidly progressive encephalopathy manifesting in susceptibile individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem. Note=Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (PubMed:19118815).<ref>PMID:19118815</ref>
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==Reference==
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== Function ==
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<references group="xtra"/><references/>
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[https://www.uniprot.org/uniprot/RBP2_HUMAN RBP2_HUMAN] E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Could also have isomerase or chaperone activity and may bind RNA or DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1.<ref>PMID:11792325</ref> <ref>PMID:12032081</ref> <ref>PMID:15378033</ref> <ref>PMID:15931224</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Hoelz, A.]]
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[[Category: Large Structures]]
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[[Category: Kassube, S A.]]
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[[Category: Hoelz A]]
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[[Category: Lin, D H.]]
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[[Category: Kassube SA]]
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[[Category: Stuwe, T.]]
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[[Category: Lin DH]]
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[[Category: Nuclear pore complex component nucleocytoplasmic transport]]
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[[Category: Stuwe T]]
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[[Category: Tpr motif]]
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[[Category: Transport protein]]
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Current revision

Structure of the N-terminal domain of Nup358

PDB ID 4ga0

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