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1chl

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Revision as of 10:37, 14 July 2021

NMR SEQUENTIAL ASSIGNMENTS AND SOLUTION STRUCTURE OF CHLOROTOXIN, A SMALL SCORPION TOXIN THAT BLOCKS CHLORIDE CHANNELS

Structural highlights

1chl is a 1 chain structure with sequence from Egyptian scorpion. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CTXL_LEIQU] This toxin binds to the surface of glioma cells, and inhibits their proliferation without having effects on normal brain cells. In this context, this toxin has been described as a chloride channel inhibitor (probably ClC-3/CLCN3) by causing its internalization via caveolae (PubMed:16520829). It has also been described to selectively interact with MMP2 (in complex with MT1-MMP (MMP14) and TIMP2), to inhibit its enzymatic activity and to decrease its presence at the cell surface (PubMed:12454020).^[1] ^[2] ^[3]

Publication Abstract from PubMed

The solution structure of chlorotoxin, a small toxin purified from the venom of the Leiurus quinquestriatus scorpion, has been determined using 2D 1H NMR spectroscopy. Analysis of the NMR data shows that the structure consists of a small three-stranded antiparallel beta-sheet packed against an alpha-helix, thereby adopting the same fold as charybdotoxin and other members of the short scorpion toxin family [Arseniev et al. (1984) FEBS Lett. 165, 57-62; Martins et al. (1990) FEBS Lett. 260, 249-253; Bontems et al. (1991) Science 254, 1521-1523]. Three disulfide bonds of chlorotoxin (Cys5-Cys28, Cys16-Cys33, and Cys20-Cys35), cross-linking the alpha-helix to the beta-sheet, follow the common pattern found in the other short scorpion toxins. The fourth disulfide bridge (Cys2-Cys19) links the small N-terminal beta strand to the rest of the molecule, in contrast to charybdotoxin where this disulfide bridge is absent and the first strand interacts with the rest of the molecule by several contacts between hydrophobic residues. Another structural difference between chlorotoxin and charybdotoxin is observed at the level of the alpha-beta turn. This difference is accompanied by a change in the electrostatic potential surface, which is largely positive at the level of this turn in chlorotoxin, whereas no such positive potential surface can be found at the same position in charybdotoxin. In the latter protein, the positive surface is formed by different charged residues situated on the solvent-exposed site of the C-terminal beta-sheet.(ABSTRACT TRUNCATED AT 250 WORDS)

NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels.,Lippens G, Najib J, Wodak SJ, Tartar A Biochemistry. 1995 Jan 10;34(1):13-21. PMID:7819188^[4]

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

References

↑ Deshane J, Garner CC, Sontheimer H. Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2. J Biol Chem. 2003 Feb 7;278(6):4135-44. Epub 2002 Nov 25. PMID:12454020 doi:http://dx.doi.org/10.1074/jbc.M205662200
↑ McFerrin MB, Sontheimer H. A role for ion channels in glioma cell invasion. Neuron Glia Biol. 2006 Feb;2(1):39-49. PMID:16520829 doi:http://dx.doi.org/10.1017/S17440925X06000044
↑ DeBin JA, Maggio JE, Strichartz GR. Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion. Am J Physiol. 1993 Feb;264(2 Pt 1):C361-9. PMID:8383429
↑ Lippens G, Najib J, Wodak SJ, Tartar A. NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels. Biochemistry. 1995 Jan 10;34(1):13-21. PMID:7819188

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1chl' size='340' side='right'caption='[[1chl]], [[NMR_Ensembles_of_Models | 7 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1chl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Egyptian_scorpion Egyptian scorpion]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CHL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1chl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Egyptian_scorpion Egyptian scorpion]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHL 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=1chl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chl OCA], [http://pdbe.org/1chl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1chl RCSB], [http://www.ebi.ac.uk/pdbsum/1chl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1chl 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=1chl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chl OCA], [https://pdbe.org/1chl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chl RCSB], [https://www.ebi.ac.uk/pdbsum/1chl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CTXL_LEIQU CTXL_LEIQU]] This toxin binds to the surface of glioma cells, and inhibits their proliferation without having effects on normal brain cells. In this context, this toxin has been described as a chloride channel inhibitor (probably ClC-3/CLCN3) by causing its internalization via caveolae (PubMed:16520829). It has also been described to selectively interact with MMP2 (in complex with MT1-MMP (MMP14) and TIMP2), to inhibit its enzymatic activity and to decrease its presence at the cell surface (PubMed:12454020).<ref>PMID:12454020</ref> <ref>PMID:16520829</ref> <ref>PMID:8383429</ref>
+[[https://www.uniprot.org/uniprot/CTXL_LEIQU CTXL_LEIQU]] This toxin binds to the surface of glioma cells, and inhibits their proliferation without having effects on normal brain cells. In this context, this toxin has been described as a chloride channel inhibitor (probably ClC-3/CLCN3) by causing its internalization via caveolae (PubMed:16520829). It has also been described to selectively interact with MMP2 (in complex with MT1-MMP (MMP14) and TIMP2), to inhibit its enzymatic activity and to decrease its presence at the cell surface (PubMed:12454020).<ref>PMID:12454020</ref> <ref>PMID:16520829</ref> <ref>PMID:8383429</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1chl

From Proteopedia

Revision as of 10:37, 14 July 2021

NMR SEQUENTIAL ASSIGNMENTS AND SOLUTION STRUCTURE OF CHLOROTOXIN, A SMALL SCORPION TOXIN THAT BLOCKS CHLORIDE CHANNELS

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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