1chl
From Proteopedia
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</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://www.rcsb.org/pdb/explore.do?structureId=1chl RCSB], [http://www.ebi.ac.uk/pdbsum/1chl PDBsum]</span></td></tr> | </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://www.rcsb.org/pdb/explore.do?structureId=1chl RCSB], [http://www.ebi.ac.uk/pdbsum/1chl PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SCXL_LEIQU SCXL_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:8383429</ref> <ref>PMID:12454020</ref> <ref>PMID:16520829</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 07:38, 24 December 2014
NMR SEQUENTIAL ASSIGNMENTS AND SOLUTION STRUCTURE OF CHLOROTOXIN, A SMALL SCORPION TOXIN THAT BLOCKS CHLORIDE CHANNELS
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