1qgr

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(New page: 200px<br /> <applet load="1qgr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qgr, resolution 2.3&Aring;" /> '''STRUCTURE OF IMPORTI...)
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[[Image:1qgr.gif|left|200px]]<br />
 
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<applet load="1qgr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qgr, resolution 2.3&Aring;" />
 
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'''STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)'''<br />
 
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==Overview==
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==STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)==
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Cytosolic proteins bearing a classical nuclear localization signal enter, the nucleus bound to a heterodimer of importin-alpha and importin-beta, (also called karyopherin-alpha and -beta). The formation of this, heterodimer involves the importin-beta-binding (IBB) domain of, importin-alpha, a highly basic amino-terminal region of roughly 40, amino-acid residues. Here we report the crystal structure of human, importin-beta bound to the IBB domain of importin-alpha, determined at 2.5, A and 2.3 A resolution in two crystal forms. Importin-beta consists of 19, tandemly repeated HEAT motifs and wraps intimately around the IBB domain., The association involves two separate regions of importin-beta, recognizing structurally distinct parts of the IBB domain: an, amino-terminal extended moiety and a carboxy-terminal helix. The structure, indicates that significant conformational changes occur when importin-beta, binds or releases the IBB domain domain and suggests how dissociation of, the importin-alpha/beta heterodimer may be achieved upon nuclear entry.
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<StructureSection load='1qgr' size='340' side='right'caption='[[1qgr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qgr]] 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=1QGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QGR 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]] 2.3&#8491;</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=1qgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgr OCA], [https://pdbe.org/1qgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qgr RCSB], [https://www.ebi.ac.uk/pdbsum/1qgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qgr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IMB1_HUMAN IMB1_HUMAN] Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats 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 importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. 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. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports PRKCI into the nucleus.<ref>PMID:9687515</ref> <ref>PMID:10228156</ref> <ref>PMID:11891849</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/qg/1qgr_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=1qgr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-alpha and importin-beta (also called karyopherin-alpha and -beta). The formation of this heterodimer involves the importin-beta-binding (IBB) domain of importin-alpha, a highly basic amino-terminal region of roughly 40 amino-acid residues. Here we report the crystal structure of human importin-beta bound to the IBB domain of importin-alpha, determined at 2.5 A and 2.3 A resolution in two crystal forms. Importin-beta consists of 19 tandemly repeated HEAT motifs and wraps intimately around the IBB domain. The association involves two separate regions of importin-beta, recognizing structurally distinct parts of the IBB domain: an amino-terminal extended moiety and a carboxy-terminal helix. The structure indicates that significant conformational changes occur when importin-beta binds or releases the IBB domain domain and suggests how dissociation of the importin-alpha/beta heterodimer may be achieved upon nuclear entry.
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==About this Structure==
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Structure of importin-beta bound to the IBB domain of importin-alpha.,Cingolani G, Petosa C, Weis K, Muller CW Nature. 1999 May 20;399(6733):221-9. PMID:10353244<ref>PMID:10353244</ref>
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1QGR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QGR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of importin-beta bound to the IBB domain of importin-alpha., Cingolani G, Petosa C, Weis K, Muller CW, Nature. 1999 May 20;399(6733):221-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10353244 10353244]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1qgr" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Cingolani, G.]]
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[[Category: Muller, C.W.]]
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[[Category: Petosa, C.]]
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[[Category: Weis, K.]]
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[[Category: heat motif]]
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[[Category: nls-binding]]
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[[Category: nuclear import]]
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[[Category: transport receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:53:03 2007''
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==See Also==
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*[[Importin 3D structures|Importin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cingolani G]]
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[[Category: Muller CW]]
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[[Category: Petosa C]]
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[[Category: Weis K]]

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STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)

PDB ID 1qgr

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