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1ter
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=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [http://www.ebi.ac.uk/pdbsum/1ter 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=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [http://www.ebi.ac.uk/pdbsum/1ter PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TERT_APIME TERT_APIME]] Presynaptic neurotoxin that blocks the inwardly rectifying Kir1.1/KCNJ1 and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. It may block the potassium channel pore by occluding its alpha helix into the channel vestibule. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimers potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh), because these channels are activated by ACh) are found in mammalian myocytes. Interacts specifically with calmodulin in the presence of calcium.<ref>PMID:9748337</ref> <ref>PMID:6091685</ref> <ref>PMID:10572004</ref> <ref>PMID:11015309</ref> <ref>PMID:10734170</ref> <ref>PMID:15947038</ref> <ref>PMID:16725344</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 17:39, 24 December 2014
SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY
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