3rz9

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==Mouse importin alpha-Ku80 NLS peptide complex==
==Mouse importin alpha-Ku80 NLS peptide complex==
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<StructureSection load='3rz9' size='340' side='right' caption='[[3rz9]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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<StructureSection load='3rz9' size='340' side='right'caption='[[3rz9]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rz9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RZ9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rz9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RZ9 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l3q|3l3q]], [[1q1s|1q1s]], [[1q1t|1q1t]], [[1ejl|1ejl]]</td></tr>
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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]] 2.29&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3rz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rz9 OCA], [https://pdbe.org/3rz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rz9 RCSB], [https://www.ebi.ac.uk/pdbsum/3rz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rz9 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rz9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rz9 RCSB], [http://www.ebi.ac.uk/pdbsum/3rz9 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/IMA1_MOUSE IMA1_MOUSE] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. 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.
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== Publication Abstract from PubMed ==
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Ku70 and Ku80 form a heterodimeric complex involved in multiple nuclear processes. This complex plays a key role in DNA repair due to its ability to bind DNA double-strand breaks and facilitate repair by the nonhomologous end-joining pathway. Ku70 and Ku80 have been proposed to contain bipartite and monopartite nuclear localization sequences (NLSs), respectively, that allow them to be translocated to the nucleus independently of each other via the classical importin-alpha (Impalpha)/importin-beta-mediated nuclear import pathway. To determine the structural basis of the recognition of Ku70 and Ku80 proteins by Impalpha, we solved the crystal structures of the complexes of Impalpha with the peptides corresponding to the Ku70 and Ku80 NLSs. Our structural studies confirm the binding of the Ku80 NLS as a classical monopartite NLS but reveal an unexpected binding mode for Ku70 NLS with only one basic cluster bound to the receptor. Both Ku70 and Ku80 therefore contain monopartite NLSs, and sequences outside the basic cluster make favorable interactions with Impalpha, suggesting that this may be a general feature in monopartite NLSs. We show that the Ku70 NLS has a higher affinity for Impalpha than the Ku80 NLS, consistent with more extensive interactions in its N-terminal region. The prospect of nuclear import of Ku70 and Ku80 independently of each other provides a powerful regulatory mechanism for the function of the Ku70/Ku80 heterodimer and independent functions of the two proteins.
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Structural basis of importin-alpha-mediated nuclear transport for Ku70 and Ku80.,Takeda AA, de Barros AC, Chang CW, Kobe B, Fontes MR J Mol Biol. 2011 Sep 16;412(2):226-34. Epub 2011 Jul 23. PMID:21806995<ref>PMID:21806995</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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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__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Barros, A C.]]
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[[Category: Barros AC]]
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[[Category: Fontes, M R.M.]]
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[[Category: Fontes MRM]]
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[[Category: Takeda, A A.S.]]
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[[Category: Takeda AAS]]
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[[Category: Armadillo repeat]]
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[[Category: Protein transport]]
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Mouse importin alpha-Ku80 NLS peptide complex

PDB ID 3rz9

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