5yu6: Difference between revisions

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'''Unreleased structure'''


The entry 5yu6 is ON HOLD
==CRYSTAL STRUCTURE OF EXPORTIN-5:RANGTP COMPLEX==
<StructureSection load='5yu6' size='340' side='right'caption='[[5yu6]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yu6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YU6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.997&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5yu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yu6 OCA], [https://pdbe.org/5yu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yu6 RCSB], [https://www.ebi.ac.uk/pdbsum/5yu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yu6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XPO5_HUMAN XPO5_HUMAN] Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner.<ref>PMID:12426392</ref> <ref>PMID:11777942</ref> <ref>PMID:12426393</ref> <ref>PMID:14681208</ref> <ref>PMID:12509441</ref> <ref>PMID:14570900</ref> <ref>PMID:15254228</ref> <ref>PMID:14730017</ref> <ref>PMID:14631048</ref> <ref>PMID:15613540</ref> <ref>PMID:19124606</ref>  Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference, and adenovirus VA1 dsRNA. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP.<ref>PMID:12426392</ref> <ref>PMID:11777942</ref> <ref>PMID:12426393</ref> <ref>PMID:14681208</ref> <ref>PMID:12509441</ref> <ref>PMID:14570900</ref> <ref>PMID:15254228</ref> <ref>PMID:14730017</ref> <ref>PMID:14631048</ref> <ref>PMID:15613540</ref> <ref>PMID:19124606</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the nucleus, RanGTP binding to importin dissociates the cargo. On the other hand, RanGTP enables exportin to bind export cargo and form the export complex by each exportin's own cargo selection mechanism. Here, we present two X-ray structures for Exportin-5 (Exp-5) alone and Exp-5:RanGTP intermediate complex. The structure of Exp-5 adopts a ring-shaped closed conformation by C-terminal anchor residues 1,167-1,179, interacting with N-terminal heat repeats 4-9. The closed form of Exp-5 is important for the stability of the cargo-free state. Interaction between Exp-5 and RanGTP induces elimination of intramolecular contacts of the C-terminal anchor. A large movement of N-terminal 1-9th heat repeats and C-terminal 19-20th heat repeats creates an open space for RanGTP accommodation. Exp-5 in Exp-5:RanGTP and Exp-5:RanGTP:pre-miRNA adopts the same conformation. RanGTP binding to Exp-5 creates a selective molecular cage area for accepting its cargoes, such as small double-stranded RNAs, without conformational change in Exp-5:RanGTP.


Authors: Yamazawa, R., Jiko, C., Lee, S.J., Yamashita, E.
Structural Basis for Selective Binding of Export Cargoes by Exportin-5.,Yamazawa R, Jiko C, Choi S, Park IY, Nakagawa A, Yamashita E, Lee SJ Structure. 2018 Jul 16. pii: S0969-2126(18)30246-6. doi:, 10.1016/j.str.2018.06.014. PMID:30100359<ref>PMID:30100359</ref>


Description: CRYSTAL STRUCTURE OF EXPORTIN-5:RANGTP COMPLEX
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Yamashita, E]]
<div class="pdbe-citations 5yu6" style="background-color:#fffaf0;"></div>
[[Category: Lee, S.J]]
 
[[Category: Yamazawa, R]]
==See Also==
[[Category: Jiko, C]]
*[[Exportin 3D structures|Exportin 3D structures]]
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canis lupus familiaris]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Unidentified]]
[[Category: Jiko C]]
[[Category: Lee SJ]]
[[Category: Yamashita E]]
[[Category: Yamazawa R]]

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