2p8q: Difference between revisions

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[[Image:2p8q.jpg|left|200px]]


{{Structure
==Crystal Structure of human Importin beta bound to the Snurportin1 IBB-domain==
|PDB= 2p8q |SIZE=350|CAPTION= <scene name='initialview01'>2p8q</scene>, resolution 2.35&Aring;
<StructureSection load='2p8q' size='340' side='right'caption='[[2p8q]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2p8q]] 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=2P8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P8Q FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
|GENE= KPNB1, NTF97 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p8q OCA], [https://pdbe.org/2p8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p8q RCSB], [https://www.ebi.ac.uk/pdbsum/2p8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p8q ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[1qgk|1QGK]], [[1ukl|1UKL]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p8q OCA], [http://www.ebi.ac.uk/pdbsum/2p8q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p8q RCSB]</span>
[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>
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p8/2p8q_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2p8q ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nuclear import of uridine-rich ribonucleoproteins is mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin alpha, SNP1 uses an N-terminal importin beta binding (sIBB) domain to recruit the receptor importin beta and gain access to the nucleus. In this study, we demonstrate that the sIBB domain has a bipartite nature, which contains two distinct binding determinants for importin beta. The first determinant spans residues 25-65 and includes the previously identified importin alpha IBB (alphaIBB) region of homology. The second binding determinant encompasses residues 1-24 and resembles region 1011-1035 of the nucleoporin 153 (Nup153). The two binding determinants synergize within the sIBB domain to confer a low nanomolar binding affinity for importin beta (K(d) approximately 2 nm) in an interaction that, in vitro, is displaced by RanGTP. We propose that in vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of uridine-rich ribonucleoproteins into the nucleus.


'''Crystal Structure of human Importin beta bound to the Snurportin1 IBB-domain'''
Molecular basis for the recognition of snurportin 1 by importin beta.,Mitrousis G, Olia AS, Walker-Kopp N, Cingolani G J Biol Chem. 2008 Mar 21;283(12):7877-84. Epub 2008 Jan 9. PMID:18187419<ref>PMID:18187419</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2p8q" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The nuclear import of uridine-rich ribonucleoproteins (U snRNPs) is mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin alpha, SNP1 uses an N-terminal importin beta binding (sIBB) domain to recruit the receptor importin beta and gain access to the nucleus. In this paper, we demonstrate the sIBB-domain has a bipartite nature, which contains two distinct binding determinants for importin beta. The first determinant spans residues 25-65, and includes the previously identified alphaIBB-region of homology. The second binding determinant encompasses residues 1-24 and resembles region 1011-1035 of the nucleoporin 153 (Nup153). The two binding determinants synergize within the sIBB-domain to confer a low nanomolar binding affinity for importin beta, (Kd ~2nM) in an interaction that, in vitro, is displaced by RanGppNHp. We propose that in vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of U snRNPs into the nucleus.
*[[Importin 3D structures|Importin 3D structures]]
 
== References ==
==About this Structure==
<references/>
2P8Q is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P8Q OCA].
__TOC__
 
</StructureSection>
==Reference==
Molecular basis for the recognition of snurportin 1 by importin beta., Mitrousis G, Olia AS, Walker-Kopp N, Cingolani G, J Biol Chem. 2008 Jan 9;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18187419 18187419]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Cingolani, G.]]
[[Category: Cingolani G]]
[[Category: Mitrousis, G.]]
[[Category: Mitrousis G]]
[[Category: heat repeat]]
[[Category: ibb-domain]]
[[Category: importin]]
[[Category: karyopherin]]
[[Category: protein transport]]
[[Category: snurportin]]
 
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