1ter: Difference between revisions
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==SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY== | ==SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY== | ||
<StructureSection load='1ter' size='340' side='right'caption='[[1ter | <StructureSection load='1ter' size='340' side='right'caption='[[1ter]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ter]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ter]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TER FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [https://pdbe.org/1ter PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [https://www.ebi.ac.uk/pdbsum/1ter PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ter ProSAT]</span></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=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [https://pdbe.org/1ter PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [https://www.ebi.ac.uk/pdbsum/1ter PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ter ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://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 == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Apis mellifera]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Nelson | [[Category: Nelson JW]] | ||
[[Category: Xu | [[Category: Xu X]] | ||