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[[Image:3oqs.jpg|left|200px]]
==Crystal structure of importin-alpha bound to a CLIC4 NLS peptide==
<StructureSection load='3oqs' size='340' side='right' caption='[[3oqs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3oqs]] 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=3OQS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OQS FirstGlance]. <br>
</td></tr><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>
<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=3oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oqs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oqs RCSB], [http://www.ebi.ac.uk/pdbsum/3oqs PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
It has been reported that a human chloride intracellular channel (CLIC) protein, CLIC4, translocates to the nucleus in response to cellular stress, facilitated by a putative CLIC4 nuclear localization signal (NLS). The CLIC4 NLS adopts an alpha-helical structure in the native CLIC4 fold. It is proposed that CLIC4 is transported to the nucleus via the classical nuclear import pathway after binding the import receptor, importin-alpha. In this study, we have determined the X-ray crystal structure of a truncated form of importin-alpha lacking the importin-beta binding domain, bound to a CLIC4 NLS peptide. The NLS peptide binds to the major binding site in an extended conformation similar to that observed for the classical simian virus 40 large T-antigen NLS. A Tyr residue within the CLIC4 NLS makes surprisingly favourable interactions by forming side-chain hydrogen bonds to the importin-alpha backbone. This structural evidence supports the hypothesis that CLIC4 translocation to the nucleus is governed by the importin-alpha nuclear import pathway, provided that CLIC4 can undergo a conformational rearrangement that exposes the NLS in an extended conformation.


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Crystal structure of importin-alpha bound to a peptide bearing the nuclear localisation signal from chloride intracellular channel protein 4.,Mynott AV, Harrop SJ, Brown LJ, Breit SN, Kobe B, Curmi PM FEBS J. 2011 May;278(10):1662-75. doi: 10.1111/j.1742-4658.2011.08086.x., Epub 2011 Mar 30. PMID:21388519<ref>PMID:21388519</ref>
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{{STRUCTURE_3oqs|  PDB=3oqs  |  SCENE=  }}


===Crystal structure of importin-alpha bound to a CLIC4 NLS peptide===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
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{{ABSTRACT_PUBMED_21388519}}
 
==About this Structure==
[[3oqs]] 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=3OQS OCA].
 
==Reference==
<ref group="xtra">PMID:021388519</ref><references group="xtra"/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Brown, L J.]]
[[Category: Brown, L J.]]

Revision as of 10:22, 28 May 2014

Crystal structure of importin-alpha bound to a CLIC4 NLS peptide

3oqs, resolution 2.00Å

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