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1tyk
From Proteopedia
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<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=1tyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tyk RCSB], [http://www.ebi.ac.uk/pdbsum/1tyk PDBsum]</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=1tyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tyk RCSB], [http://www.ebi.ac.uk/pdbsum/1tyk PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MTX4_GRASP MTX4_GRASP]] This cationic hydrophobic peptide inhibits a lot of different channels and has an antimicrobial activity. It blocks mechanosensitive ion channels (also named stretch-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents. Acts by partitioning into the membrane and perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. Inhibits atrial fibrillation as well as the membrane motor of outer hair cells at low doses. It also binds to the voltage sensor of voltage-gated potassium channels from the archaebacterium Aeropyrum pernix (KvAP) without affecting channel gating. It has also a medium toxicity on a large spectra of sodium channels (Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A, Nav1.7/SCN9A), and also inhibits potassium channels Kv11.1/KCNH2 and Kv11.2/KCNH6. It also exhibits antimicrobial activities against the Gram-positive bacteria B.subtilis (MIC=0.5 uM), S.aureus (MIC=2-4 uM), and S.epidermidis (MIC=4-8 uM), and Gram-negative bacteria S.typhimurium (MIC=32.64 uM), P.aeruginosa (MIC=8-16 uM), and E.coli (MIC=8-16 uM).<ref>PMID:10779316</ref> <ref>PMID:19955179</ref> <ref>PMID:11343101</ref> <ref>PMID:15287735</ref> <ref>PMID:15241420</ref> <ref>PMID:16376854</ref> <ref>PMID:16797839</ref> <ref>PMID:17384064</ref> <ref>PMID:17573432</ref> | ||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 22:29, 24 December 2014
SOLUTION STRUCTURE OF A TOXIN FROM THE TARANTULA, GRAMMOSTOLA SPATULATA, WHICH INHIBITS MECHANOSENSITIVE ION CHANNELS
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