7m1e: Difference between revisions
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==Structural and functional studies about scorpine showed the presence of blocking channel and cytolytic activities as well as two different structural domains== | |||
<StructureSection load='7m1e' size='340' side='right'caption='[[7m1e]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7m1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pandinus_imperator Pandinus imperator]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M1E FirstGlance]. <br> | |||
</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=7m1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m1e OCA], [https://pdbe.org/7m1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m1e RCSB], [https://www.ebi.ac.uk/pdbsum/7m1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m1e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KBX3_PANIM KBX3_PANIM] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Scorpine is an antimicrobial and antimalarial peptide isolated from Pandinus imperator scorpion venom. As there are few functional and structural studies reported on scorpine-like peptides, we investigated the recombinant truncated N- and C-terminal domains as well as complete scorpine using biological assays and determined the N- and C-terminal structures using solution nuclear magnetic resonance. The study was conducted using recombinant N- and C-terminal peptides and complete scorpine expressed in Escherichia coli. The results showed that N-scorpine presented a random coil structure in water and adopted alpha-helical folding in the presence of 50% trifluoroethanol (TFE). C-scorpine contains three disulfide bonds with two structural domains: an unstructured N-terminal domain in water that can form a typical secondary alpha-helix structure in 50% TFE and a C-terminal domain with the CS-alphabeta motif. Our findings demonstrate cytolytic activity associated with C-scorpine, N-scorpine, and scorpine, as well as channel blocking activity associated with the C-scorpine domain. | |||
Structural and functional studies of scorpine: A channel blocker and cytolytic peptide.,Lopez-Giraldo E, Carrillo E, Titaux-Delgado G, Cano-Sanchez P, Colorado A, Possani LD, Rio-Portilla FD Toxicon. 2022 Nov 24;222:106985. doi: 10.1016/j.toxicon.2022.106985. PMID:36436588<ref>PMID:36436588</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7m1e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pandinus imperator]] | |||
[[Category: Lopez AE]] | |||
[[Category: Titaux G]] | |||
[[Category: Del Rio JF]] | |||