3oqs: Difference between revisions

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<StructureSection load='3oqs' size='340' side='right'caption='[[3oqs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3oqs' size='340' side='right'caption='[[3oqs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3oqs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3OQS FirstGlance]. <br>
<table><tr><td colspan='2'>[[3oqs]] 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=3OQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OQS FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kpna2, Rch1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
</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&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oqs OCA], [https://pdbe.org/3oqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oqs RCSB], [https://www.ebi.ac.uk/pdbsum/3oqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oqs ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oqs OCA], [https://pdbe.org/3oqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oqs RCSB], [https://www.ebi.ac.uk/pdbsum/3oqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oqs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CLIC4_HUMAN CLIC4_HUMAN]] Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis).<ref>PMID:12163372</ref> <ref>PMID:14569596</ref> <ref>PMID:16239224</ref> <ref>PMID:18302930</ref> <ref>PMID:19247789</ref> <ref>PMID:16176272</ref> [[https://www.uniprot.org/uniprot/IMA2_MOUSE IMA2_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.
[https://www.uniprot.org/uniprot/CLIC4_HUMAN CLIC4_HUMAN] Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis).<ref>PMID:12163372</ref> <ref>PMID:14569596</ref> <ref>PMID:16239224</ref> <ref>PMID:18302930</ref> <ref>PMID:19247789</ref> <ref>PMID:16176272</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Brown, L J]]
[[Category: Brown LJ]]
[[Category: Curmi, P M.G]]
[[Category: Curmi PMG]]
[[Category: Harrop, S J]]
[[Category: Harrop SJ]]
[[Category: Mynott, A V]]
[[Category: Mynott AV]]
[[Category: Armadillo repeat]]
[[Category: Chloride intracellular channel 4]]
[[Category: Clic4 nl]]
[[Category: Importin alpha]]
[[Category: Karyopherin alpha]]
[[Category: Nuclear import]]
[[Category: Protein transport]]

Latest revision as of 19:56, 1 November 2023

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

Structural highlights

3oqs is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CLIC4_HUMAN Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis).[1] [2] [3] [4] [5] [6]

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.

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[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Ronnov-Jessen L, Villadsen R, Edwards JC, Petersen OW. Differential expression of a chloride intracellular channel gene, CLIC4, in transforming growth factor-beta1-mediated conversion of fibroblasts to myofibroblasts. Am J Pathol. 2002 Aug;161(2):471-80. PMID:12163372
  2. ↑ Berryman MA, Goldenring JR. CLIC4 is enriched at cell-cell junctions and colocalizes with AKAP350 at the centrosome and midbody of cultured mammalian cells. Cell Motil Cytoskeleton. 2003 Nov;56(3):159-72. PMID:14569596 doi:http://dx.doi.org/10.1002/cm.10141
  3. ↑ Bohman S, Matsumoto T, Suh K, Dimberg A, Jakobsson L, Yuspa S, Claesson-Welsh L. Proteomic analysis of vascular endothelial growth factor-induced endothelial cell differentiation reveals a role for chloride intracellular channel 4 (CLIC4) in tubular morphogenesis. J Biol Chem. 2005 Dec 23;280(51):42397-404. Epub 2005 Oct 20. PMID:16239224 doi:http://dx.doi.org/10.1074/jbc.M506724200
  4. ↑ Maeda K, Haraguchi M, Kuramasu A, Sato T, Ariake K, Sakagami H, Kondo H, Yanai K, Fukunaga K, Yanagisawa T, Sukegawa J. CLIC4 interacts with histamine H3 receptor and enhances the receptor cell surface expression. Biochem Biophys Res Commun. 2008 May 2;369(2):603-8. Epub 2008 Feb 25. PMID:18302930 doi:http://dx.doi.org/S0006-291X(08)00320-3
  5. ↑ Tung JJ, Hobert O, Berryman M, Kitajewski J. Chloride intracellular channel 4 is involved in endothelial proliferation and morphogenesis in vitro. Angiogenesis. 2009;12(3):209-20. doi: 10.1007/s10456-009-9139-3. Epub 2009 Feb, 27. PMID:19247789 doi:http://dx.doi.org/10.1007/s10456-009-9139-3
  6. ↑ Littler DR, Assaad NN, Harrop SJ, Brown LJ, Pankhurst GJ, Luciani P, Aguilar MI, Mazzanti M, Berryman MA, Breit SN, Curmi PM. Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4. FEBS J. 2005 Oct;272(19):4996-5007. PMID:16176272 doi:10.1111/j.1742-4658.2005.04909.x
  7. ↑ Mynott AV, Harrop SJ, Brown LJ, Breit SN, Kobe B, Curmi PM. Crystal structure of importin-alpha bound to a peptide bearing the nuclear localisation signal from chloride intracellular channel protein 4. FEBS J. 2011 May;278(10):1662-75. doi: 10.1111/j.1742-4658.2011.08086.x., Epub 2011 Mar 30. PMID:21388519 doi:10.1111/j.1742-4658.2011.08086.x

3oqs, resolution 2.00Å

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