3ww0

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Current revision (08:47, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3ww0' size='340' side='right'caption='[[3ww0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3ww0' size='340' side='right'caption='[[3ww0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ww0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WW0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ww0]] 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=3WW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WW0 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wvz|3wvz]]</div></td></tr>
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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]] 2.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C11orf73, HSPC138, HSPC179, HSPC248 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ww0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ww0 OCA], [https://pdbe.org/3ww0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ww0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ww0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ww0 ProSAT]</span></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=3ww0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ww0 OCA], [https://pdbe.org/3ww0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ww0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ww0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ww0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HIKES_HUMAN HIKES_HUMAN]] Acts as a specific nuclear import carrier for HSP70 proteins following heat-shock stress: acts by mediating the nucleoporin-dependent translocation of ATP-bound HSP70 proteins into the nucleus. HSP70 proteins import is required to protect cells from heat shock damages. Does not translocate ADP-bound HSP70 proteins into the nucleus.<ref>PMID:22541429</ref>
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[https://www.uniprot.org/uniprot/HIKES_HUMAN HIKES_HUMAN] Acts as a specific nuclear import carrier for HSP70 proteins following heat-shock stress: acts by mediating the nucleoporin-dependent translocation of ATP-bound HSP70 proteins into the nucleus. HSP70 proteins import is required to protect cells from heat shock damages. Does not translocate ADP-bound HSP70 proteins into the nucleus.<ref>PMID:22541429</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hikeshi is a nuclear transport receptor required for cell survival after stress. It mediates heat-shock-induced nuclear import of 70 kDa heat-shock proteins (Hsp70s) through interactions with FG-nucleoporins (FG-Nups), which are proteins in nuclear pore complexes (NPCs). Here, the crystal structure of human Hikeshi is presented at 1.8 A resolution. Hikeshi forms an asymmetric homodimer that is responsible for the interaction with Hsp70s. The asymmetry of Hikeshi arises from the distinct conformation of the C-terminal domain (CTD) and the flexibility of the linker regions of each monomer. Structure-guided mutational analyses showed that both the flexible linker region and the CTD are important for nuclear import of Hsp70. Pull-down assays revealed that only full-length Hsp70s can interact with Hikeshi. The N-terminal domain (NTD) consists of a jelly-roll/beta-sandwich fold structure which contains hydrophobic pockets involved in FG-Nup recognition. A unique extended loop (E-loop) in the NTD is likely to regulate the interactions of Hikeshi with FG-Nups. The crystal structure of Hikeshi explains how Hikeshi participates in the regulation of nuclear import through the recognition of FG-Nups and which part of Hikeshi affects its binding to Hsp70. This study is the first to yield structural insight into this highly unique import receptor.
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Structural and functional analysis of Hikeshi, a new nuclear transport receptor of Hsp70s.,Song J, Kose S, Watanabe A, Son SY, Choi S, Hong H, Yamashita E, Park IY, Imamoto N, Lee SJ Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):473-83. doi:, 10.1107/S1399004714026881. Epub 2015 Feb 26. PMID:25760597<ref>PMID:25760597</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ww0" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Choi, S]]
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[[Category: Choi S]]
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[[Category: Hong, R H]]
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[[Category: Hong RH]]
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[[Category: Imamoto, N]]
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[[Category: Imamoto N]]
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[[Category: Kose, S]]
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[[Category: Kose S]]
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[[Category: Lee, S J]]
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[[Category: Lee SJ]]
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[[Category: Park, I Y]]
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[[Category: Park IY]]
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[[Category: Son, S Y]]
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[[Category: Son SY]]
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[[Category: Song, J]]
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[[Category: Song J]]
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[[Category: Watanabe, A]]
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[[Category: Watanabe A]]
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[[Category: Yamashita, E]]
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[[Category: Yamashita E]]
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[[Category: Nuclear transport receptor]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of F97A mutant, a new nuclear transport receptor of Hsp70

PDB ID 3ww0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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