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1qbk

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(New page: 200px<br /> <applet load="1qbk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qbk, resolution 3.0&Aring;" /> '''STRUCTURE OF THE KAR...)
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[[Image:1qbk.gif|left|200px]]<br />
 
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<applet load="1qbk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qbk, resolution 3.0&Aring;" />
 
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'''STRUCTURE OF THE KARYOPHERIN BETA2-RAN GPPNHP NUCLEAR TRANSPORT COMPLEX'''<br />
 
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==Overview==
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==STRUCTURE OF THE KARYOPHERIN BETA2-RAN GPPNHP NUCLEAR TRANSPORT COMPLEX==
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Transport factors in the karyopherin-beta (also called importin-beta), family mediate the movement of macromolecules in nuclear-cytoplasmic, transport pathways. Karyopherin-beta2 (transportin) binds a cognate import, substrate and targets it to the nuclear pore complex. In the nucleus, Ran, x GTP binds karyopherin-beta2 and dissociates the substrate. Here we, present the 3.0 A structure of the karyopherin-beta2-Ran x GppNHp complex, where GppNHp is a non-hydrolysable GTP analogue. Karyopherin-beta2, contains eighteen HEAT repeats arranged into two continuous orthogonal, arches. Ran is clamped in the amino-terminal arch and substrate-binding, activity is mapped to the carboxy-terminal arch. A large loop in HEAT, repeat 7 spans both arches. Interactions of the loop with Ran and the, C-terminal arch implicate it in GTPase-mediated dissociation of the, import-substrate. Ran x GppNHp in the complex shows extensive structural, rearrangement, compared to Ran GDP, in regions contacting, karyopherin-beta2. This provides a structural basis for the specificity of, the karyopherin-beta family for the GTP-bound state of Ran, as well as a, rationale for interactions of the karyopherin-Ran complex with the, regulatory proteins ranGAP, ranGEF and ranBP1.
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<StructureSection load='1qbk' size='340' side='right'caption='[[1qbk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qbk]] 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=1QBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QBK FirstGlance]. <br>
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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]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1qbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qbk OCA], [https://pdbe.org/1qbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qbk RCSB], [https://www.ebi.ac.uk/pdbsum/1qbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qbk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qb/1qbk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qbk ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Deafness, mitochondrial, modifier of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=610230 610230]], Osteolysis, familial expansile OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603499 603499]], Paget disease of bone OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603499 603499]]
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*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1QBK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QBK OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp., Chook YM, Blobel G, Nature. 1999 May 20;399(6733):230-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10353245 10353245]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Blobel, G.]]
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[[Category: Blobel G]]
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[[Category: Chook, Y.M.]]
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[[Category: Chook YM]]
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[[Category: GNP]]
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[[Category: MG]]
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[[Category: heat repeats]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:52:11 2007''
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Current revision

STRUCTURE OF THE KARYOPHERIN BETA2-RAN GPPNHP NUCLEAR TRANSPORT COMPLEX

PDB ID 1qbk

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