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1k0m

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Revision as of 06:47, 11 August 2021

Crystal structure of a soluble monomeric form of CLIC1 at 1.4 angstroms

Structural highlights

1k0m is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-A resolution. The protein is monomeric and structurally homologous to the glutathione S-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1-90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes.

Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.,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 J Biol Chem. 2001 Nov 30;276(48):44993-5000. Epub 2001 Sep 10. PMID:11551966^[8]

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

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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k0m"

@@ Line 3: / Line 3: @@
 <StructureSection load='1k0m' size='340' side='right'caption='[[1k0m]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1k0m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K0M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1k0m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K0M FirstGlance]. <br>
-</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=1k0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0m OCA], [http://pdbe.org/1k0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k0m RCSB], [http://www.ebi.ac.uk/pdbsum/1k0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0m ProSAT]</span></td></tr>
+</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=1k0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0m OCA], [https://pdbe.org/1k0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k0m RCSB], [https://www.ebi.ac.uk/pdbsum/1k0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0m ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1k0m

From Proteopedia

Revision as of 06:47, 11 August 2021

Crystal structure of a soluble monomeric form of CLIC1 at 1.4 angstroms

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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