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1t1t
From Proteopedia
(Difference between revisions)
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<StructureSection load='1t1t' size='340' side='right'caption='[[1t1t]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1t1t' size='340' side='right'caption='[[1t1t]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1t1t]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1t1t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Partr Partr]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T1T 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=1t1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1t OCA], [https://pdbe.org/1t1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t1t RCSB], [https://www.ebi.ac.uk/pdbsum/1t1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t1t ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/KURT_PARTR KURT_PARTR]] Alpha toxins bind voltage-independently at site-3 of sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin acts on Nav1.2/SCN2A. Also binds to Cav3.1/CACNA1G and Cav3.2/CACNA1H T-type calcium channels with high affinity and inhibits the channels by modifying voltage-dependent gating. Another study (PubMed:11896142) shows that it also targets neuronal high-threshold calcium channels, including P-type, N-type, and L-type calcium channels (Cav), and others that still are unidentified pharmacologically.<ref>PMID:10196582</ref> <ref>PMID:11896142</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:40, 22 September 2021
Solution Structure of Kurtoxin
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Categories: Large Structures | Partr | Cho, E M | Eu, Y J | Kim, J I | Kohno, T | Lee, C W | Min, H J | Cysteine stabilized alpha-beta | Toxin
