1rk4
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1rk4.png|left|200px]] | ||
| - | + | ==Crystal Structure of a Soluble Dimeric Form of Oxidised CLIC1== | |
| + | <StructureSection load='1rk4' size='340' side='right'caption='[[1rk4]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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 == | ||
| + | [[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/rk/1rk4_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1rk4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:14613939</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </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/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Bauskin | + | [[Category: Large Structures]] |
| - | [[Category: Breit | + | [[Category: Bauskin AR]] |
| - | [[Category: Brown | + | [[Category: Breit SN]] |
| - | [[Category: Campbell | + | [[Category: Brown LJ]] |
| - | [[Category: Curmi | + | [[Category: Campbell TJ]] |
| - | [[Category: DeMaere | + | [[Category: Curmi PM]] |
| - | [[Category: Fairlie | + | [[Category: DeMaere MZ]] |
| - | [[Category: Harrop | + | [[Category: Fairlie WD]] |
| - | [[Category: Littler | + | [[Category: Harrop SJ]] |
| - | [[Category: Mazzanti | + | [[Category: Littler DR]] |
| - | [[Category: Pankhurst | + | [[Category: Mazzanti M]] |
| - | [[Category: Pankhurst | + | [[Category: Pankhurst GJ]] |
| - | [[Category: Tonini | + | [[Category: Pankhurst S]] |
| - | + | [[Category: Tonini R]] | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of a Soluble Dimeric Form of Oxidised CLIC1
| |||||||||||
Categories: Homo sapiens | Large Structures | Bauskin AR | Breit SN | Brown LJ | Campbell TJ | Curmi PM | DeMaere MZ | Fairlie WD | Harrop SJ | Littler DR | Mazzanti M | Pankhurst GJ | Pankhurst S | Tonini R
