1un0

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[[Image:1un0.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Yeast Karyopherin (Importin) alpha in complex with a Nup2p N-terminal fragment==
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|PDB= 1un0 |SIZE=350|CAPTION= <scene name='initialview01'>1un0</scene>, resolution 2.60&Aring;
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<StructureSection load='1un0' size='340' side='right'caption='[[1un0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1un0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UN0 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE=
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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=1un0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un0 OCA], [https://pdbe.org/1un0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1un0 RCSB], [https://www.ebi.ac.uk/pdbsum/1un0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1un0 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1un0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un0 OCA], [http://www.ebi.ac.uk/pdbsum/1un0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1un0 RCSB]</span>
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[https://www.uniprot.org/uniprot/IMA1_YEAST IMA1_YEAST] Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).<ref>PMID:7565597</ref> <ref>PMID:10913188</ref> <ref>PMID:21075847</ref>
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}}
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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/un/1un0_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=1un0 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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The yeast nucleoporin Nup2p is associated primarily with the nuclear basket of nuclear pore complexes and is required for efficient importin-alpha:beta-mediated nuclear protein import as well as efficient nuclear export of Kap60p/importin-alpha. Residues 1-51 of Nup2p bind tightly to Kap60p and are required for Nup2p function in vivo. We have determined the 2.6 A resolution crystal structure of a complex between this region of Nup2p and the armadillo repeat domain of Kap60p. Nup2p binds along the inner concave groove of Kap60p, but its interaction interface is different from that employed for nuclear localization signal (NLS) recognition although there is some overlap between them. Nup2p binds Kap60p more strongly than NLSs and accelerates release of NLSs from Kap60p. Nup2p itself is released from Kap60p by Cse1p:RanGTP only in the presence of the importin-beta binding (IBB) domain of Kap60p. These data indicate that Nup2p increases the overall rate of nuclear trafficking by coordinating nuclear import termination and importin recycling as a concerted process.
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'''CRYSTAL STRUCTURE OF YEAST KARYOPHERIN (IMPORTIN) ALPHA IN COMPLEX WITH A NUP2P N-TERMINAL FRAGMENT'''
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Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import.,Matsuura Y, Lange A, Harreman MT, Corbett AH, Stewart M EMBO J. 2003 Oct 15;22(20):5358-69. PMID:14532109<ref>PMID:14532109</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 1un0" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The yeast nucleoporin Nup2p is associated primarily with the nuclear basket of nuclear pore complexes and is required for efficient importin-alpha:beta-mediated nuclear protein import as well as efficient nuclear export of Kap60p/importin-alpha. Residues 1-51 of Nup2p bind tightly to Kap60p and are required for Nup2p function in vivo. We have determined the 2.6 A resolution crystal structure of a complex between this region of Nup2p and the armadillo repeat domain of Kap60p. Nup2p binds along the inner concave groove of Kap60p, but its interaction interface is different from that employed for nuclear localization signal (NLS) recognition although there is some overlap between them. Nup2p binds Kap60p more strongly than NLSs and accelerates release of NLSs from Kap60p. Nup2p itself is released from Kap60p by Cse1p:RanGTP only in the presence of the importin-beta binding (IBB) domain of Kap60p. These data indicate that Nup2p increases the overall rate of nuclear trafficking by coordinating nuclear import termination and importin recycling as a concerted process.
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*[[Importin 3D structures|Importin 3D structures]]
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*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
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==About this Structure==
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== References ==
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1UN0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN0 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import., Matsuura Y, Lange A, Harreman MT, Corbett AH, Stewart M, EMBO J. 2003 Oct 15;22(20):5358-69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14532109 14532109]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Corbett, A H.]]
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[[Category: Corbett AH]]
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[[Category: Harreman, M T.]]
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[[Category: Harreman MT]]
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[[Category: Lange, A.]]
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[[Category: Lange A]]
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[[Category: Matsuura, Y.]]
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[[Category: Matsuura Y]]
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[[Category: Stewart, M.]]
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[[Category: Stewart M]]
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[[Category: armadillo repeat]]
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[[Category: karyopherin recycling]]
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[[Category: nls release]]
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[[Category: nuclear import]]
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[[Category: nucleoporin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:12:31 2008''
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Current revision

Crystal Structure of Yeast Karyopherin (Importin) alpha in complex with a Nup2p N-terminal fragment

PDB ID 1un0

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