1ie6: Difference between revisions

<table><tr><td colspan='2'>[[1ie6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IE6 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=1ie6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ie6 OCA], [http://pdbe.org/1ie6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ie6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ie6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ie6 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/IPTXA_PANIM IPTXA_PANIM]] Affects the activity of ryanodine-sensitive calcium-release channels RyR1, RyR2 and RyR3. At lower concentrations the toxin increases full openings of the RyRs, and at higher concentrations it inhibits full openings and induce openings to subconductance levels and reduces the number of full conductance openings. The different actions may be attributed to the toxins binding at different sites on the RyRs, with binding at a high-affinity site mediating the increase in full openings and the induction of subconductance states evoked upon binding to a lower-affinity site.<ref>PMID:9565405</ref> <ref>PMID:11867448</ref> <ref>PMID:14699105</ref>