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| | ==Crystal Structure of a Soluble Dimeric Form of Oxidised CLIC1== | | ==Crystal Structure of a Soluble Dimeric Form of Oxidised CLIC1== |
| - | <StructureSection load='1rk4' size='340' side='right' caption='[[1rk4]], [[Resolution|resolution]] 1.79Å' scene=''> | + | <StructureSection load='1rk4' size='340' side='right'caption='[[1rk4]], [[Resolution|resolution]] 1.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rk4]] is a 2 chain structure with sequence 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=1RK4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RK4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rk4]] 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=1RK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RK4 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k0m|1k0m]]</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]] 1.792Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLIC1, NCC27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=1rk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rk4 OCA], [https://pdbe.org/1rk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rk4 RCSB], [https://www.ebi.ac.uk/pdbsum/1rk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rk4 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rk4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rk4 RCSB], [http://www.ebi.ac.uk/pdbsum/1rk4 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CLIC1_HUMAN CLIC1_HUMAN]] Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.<ref>PMID:9139710</ref> <ref>PMID:10834939</ref> <ref>PMID:11195932</ref> <ref>PMID:11940526</ref> <ref>PMID:11978800</ref> <ref>PMID:11551966</ref> <ref>PMID:14613939</ref> | + | [https://www.uniprot.org/uniprot/CLIC1_HUMAN CLIC1_HUMAN] Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.<ref>PMID:9139710</ref> <ref>PMID:10834939</ref> <ref>PMID:11195932</ref> <ref>PMID:11940526</ref> <ref>PMID:11978800</ref> <ref>PMID:11551966</ref> <ref>PMID:14613939</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rk/1rk4_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rk/1rk4_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | + | </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=1rk4 ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 1rk4" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ion channels|Ion channels]] | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Bauskin, A R]] | + | [[Category: Large Structures]] |
| - | [[Category: Breit, S N]] | + | [[Category: Bauskin AR]] |
| - | [[Category: Brown, L J]] | + | [[Category: Breit SN]] |
| - | [[Category: Campbell, T J]] | + | [[Category: Brown LJ]] |
| - | [[Category: Curmi, P M]] | + | [[Category: Campbell TJ]] |
| - | [[Category: DeMaere, M Z]] | + | [[Category: Curmi PM]] |
| - | [[Category: Fairlie, W D]] | + | [[Category: DeMaere MZ]] |
| - | [[Category: Harrop, S J]] | + | [[Category: Fairlie WD]] |
| - | [[Category: Littler, D R]] | + | [[Category: Harrop SJ]] |
| - | [[Category: Mazzanti, M]] | + | [[Category: Littler DR]] |
| - | [[Category: Pankhurst, G J]] | + | [[Category: Mazzanti M]] |
| - | [[Category: Pankhurst, S]] | + | [[Category: Pankhurst GJ]] |
| - | [[Category: Tonini, R]] | + | [[Category: Pankhurst S]] |
| - | [[Category: Chloride ion channel]]
| + | [[Category: Tonini R]] |
| - | [[Category: Glutathione-s-tranferase superfamily]]
| + | |
| - | [[Category: Ion transport-membrane protein complex]]
| + | |
| - | [[Category: Redox-controlled structural transition]]
| + | |
| Structural highlights
Function
CLIC1_HUMAN Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Most proteins adopt a well defined three-dimensional structure; however, it is increasingly recognized that some proteins can exist with at least two stable conformations. Recently, a class of intracellular chloride ion channel proteins (CLICs) has been shown to exist in both soluble and integral membrane forms. The structure of the soluble form of CLIC1 is typical of a soluble glutathione S-transferase superfamily protein but contains a glutaredoxin-like active site. In this study we show that on oxidation CLIC1 undergoes a reversible transition from a monomeric to a non-covalent dimeric state due to the formation of an intramolecular disulfide bond (Cys-24-Cys-59). We have determined the crystal structure of this oxidized state and show that a major structural transition has occurred, exposing a large hydrophobic surface, which forms the dimer interface. The oxidized CLIC1 dimer maintains its ability to form chloride ion channels in artificial bilayers and vesicles, whereas a reducing environment prevents the formation of ion channels by CLIC1. Mutational studies show that both Cys-24 and Cys-59 are required for channel activity.
The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition.,Littler DR, Harrop SJ, Fairlie WD, Brown LJ, Pankhurst GJ, Pankhurst S, DeMaere MZ, Campbell TJ, Bauskin AR, Tonini R, Mazzanti M, Breit SN, Curmi PM J Biol Chem. 2004 Mar 5;279(10):9298-305. Epub 2003 Nov 12. PMID:14613939[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Valenzuela SM, Martin DK, Por SB, Robbins JM, Warton K, Bootcov MR, Schofield PR, Campbell TJ, Breit SN. Molecular cloning and expression of a chloride ion channel of cell nuclei. J Biol Chem. 1997 May 9;272(19):12575-82. PMID:9139710
- ↑ Tonini R, Ferroni A, Valenzuela SM, Warton K, Campbell TJ, Breit SN, Mazzanti M. Functional characterization of the NCC27 nuclear protein in stable transfected CHO-K1 cells. FASEB J. 2000 Jun;14(9):1171-8. PMID:10834939
- ↑ Valenzuela SM, Mazzanti M, Tonini R, Qiu MR, Warton K, Musgrove EA, Campbell TJ, Breit SN. The nuclear chloride ion channel NCC27 is involved in regulation of the cell cycle. J Physiol. 2000 Dec 15;529 Pt 3:541-52. PMID:11195932
- ↑ Tulk BM, Kapadia S, Edwards JC. CLIC1 inserts from the aqueous phase into phospholipid membranes, where it functions as an anion channel. Am J Physiol Cell Physiol. 2002 May;282(5):C1103-12. PMID:11940526 doi:10.1152/ajpcell.00402.2001
- ↑ Warton K, Tonini R, Fairlie WD, Matthews JM, Valenzuela SM, Qiu MR, Wu WM, Pankhurst S, Bauskin AR, Harrop SJ, Campbell TJ, Curmi PM, Breit SN, Mazzanti M. Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-dependent two-state process to form chloride ion channels with identical characteristics to those observed in Chinese hamster ovary cells expressing CLIC1. J Biol Chem. 2002 Jul 19;277(29):26003-11. Epub 2002 Apr 26. PMID:11978800 doi:http://dx.doi.org/10.1074/jbc.M203666200
- ↑ Harrop SJ, DeMaere MZ, Fairlie WD, Reztsova T, Valenzuela SM, Mazzanti M, Tonini R, Qiu MR, Jankova L, Warton K, Bauskin AR, Wu WM, Pankhurst S, Campbell TJ, Breit SN, Curmi PM. Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution. J Biol Chem. 2001 Nov 30;276(48):44993-5000. Epub 2001 Sep 10. PMID:11551966 doi:10.1074/jbc.M107804200
- ↑ Littler DR, Harrop SJ, Fairlie WD, Brown LJ, Pankhurst GJ, Pankhurst S, DeMaere MZ, Campbell TJ, Bauskin AR, Tonini R, Mazzanti M, Breit SN, Curmi PM. The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition. J Biol Chem. 2004 Mar 5;279(10):9298-305. Epub 2003 Nov 12. PMID:14613939 doi:http://dx.doi.org/10.1074/jbc.M308444200
- ↑ Littler DR, Harrop SJ, Fairlie WD, Brown LJ, Pankhurst GJ, Pankhurst S, DeMaere MZ, Campbell TJ, Bauskin AR, Tonini R, Mazzanti M, Breit SN, Curmi PM. The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition. J Biol Chem. 2004 Mar 5;279(10):9298-305. Epub 2003 Nov 12. PMID:14613939 doi:http://dx.doi.org/10.1074/jbc.M308444200
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