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| | ==Crystal structure of F97A mutant, a new nuclear transport receptor of Hsp70== | | ==Crystal structure of F97A mutant, a new nuclear transport receptor of Hsp70== |
| - | <StructureSection load='3ww0' size='340' side='right' caption='[[3ww0]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3ww0' size='340' side='right'caption='[[3ww0]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ww0]] 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=3WW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WW0 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wvz|3wvz]]</td></tr> | + | </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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C11orf73, HSPC138, HSPC179, HSPC248 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <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> |
| - | <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=3ww0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ww0 OCA], [http://pdbe.org/3ww0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ww0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ww0 PDBsum], [http://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 == |
| - | [[http://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> | + | [[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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Choi, S]] | | [[Category: Choi, S]] |
| | [[Category: Hong, R H]] | | [[Category: Hong, R H]] |
| Structural highlights
Function
[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.[1]
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kose S, Furuta M, Imamoto N. Hikeshi, a nuclear import carrier for Hsp70s, protects cells from heat shock-induced nuclear damage. Cell. 2012 Apr 27;149(3):578-89. doi: 10.1016/j.cell.2012.02.058. PMID:22541429 doi:http://dx.doi.org/10.1016/j.cell.2012.02.058
- ↑ Song J, Kose S, Watanabe A, Son SY, Choi S, Hong H, Yamashita E, Park IY, Imamoto N, Lee SJ. Structural and functional analysis of Hikeshi, a new nuclear transport receptor of Hsp70s. Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):473-83. doi:, 10.1107/S1399004714026881. Epub 2015 Feb 26. PMID:25760597 doi:http://dx.doi.org/10.1107/S1399004714026881
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