6cuc: Difference between revisions
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==Solution structure of double knot toxin (DkTx)== | ==Solution structure of double knot toxin (DkTx)== | ||
<StructureSection load='6cuc' size='340' side='right'caption='[[6cuc | <StructureSection load='6cuc' size='340' side='right'caption='[[6cuc]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cuc]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUC OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6cuc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyriopagopus_schmidti Cyriopagopus schmidti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CUC FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=6cuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cuc OCA], [https://pdbe.org/6cuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cuc RCSB], [https://www.ebi.ac.uk/pdbsum/6cuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cuc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DKTX_CYRSC DKTX_CYRSC] Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents (PubMed:20510930, PubMed:26880553, PubMed:27281200). It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein-protein interface and inserting hydrophobic residues into the bilayer (PubMed:26880553, PubMed:27281200). It also partitions naturally into membranes, with the two lobes exhibiting opposing energetics for membrane partitioning (K1) and channel activation (K2) (PubMed:26880553). In addition, the toxin disrupts a cluster of hydrophobic residues behind the selectivity filter that are critical for channel activation (PubMed:26880553).<ref>PMID:20510930</ref> <ref>PMID:26880553</ref> <ref>PMID:27281200</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cyriopagopus schmidti]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mobli | [[Category: Mobli M]] | ||
[[Category: Ramanujam | [[Category: Ramanujam V]] | ||