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==Crystal structure of human Karyopherin-beta2 bound to the histone H3 tail==
==Crystal structure of human Karyopherin-beta2 bound to the histone H3 tail==
<StructureSection load='5j3v' size='340' side='right' caption='[[5j3v]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
<StructureSection load='5j3v' size='340' side='right'caption='[[5j3v]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5j3v]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J3V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J3V FirstGlance]. <br>
<table><tr><td colspan='2'>[[5j3v]] is a 4 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=5J3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J3V FirstGlance]. <br>
</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=5j3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j3v OCA], [http://pdbe.org/5j3v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j3v RCSB], [http://www.ebi.ac.uk/pdbsum/5j3v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j3v ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.05&#8491;</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=5j3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j3v OCA], [https://pdbe.org/5j3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j3v RCSB], [https://www.ebi.ac.uk/pdbsum/5j3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j3v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TNPO1_HUMAN TNPO1_HUMAN]] Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner.<ref>PMID:8986607</ref> <ref>PMID:9687515</ref> <ref>PMID:11682607</ref> <ref>PMID:19124606</ref>
[https://www.uniprot.org/uniprot/TNPO1_HUMAN TNPO1_HUMAN] Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner.<ref>PMID:8986607</ref> <ref>PMID:9687515</ref> <ref>PMID:11682607</ref> <ref>PMID:19124606</ref>  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5j3v" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5j3v" style="background-color:#fffaf0;"></div>
==See Also==
*[[Importin 3D structures|Importin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chook, Y M]]
[[Category: Homo sapiens]]
[[Category: Soniat, M]]
[[Category: Large Structures]]
[[Category: Histone]]
[[Category: Chook YM]]
[[Category: Importin]]
[[Category: Soniat M]]
[[Category: Karyopherin]]
[[Category: Transport protein]]
[[Category: Transporting]]