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]] | |||
Latest revision as of 13:07, 21 December 2022
Structural and functional studies about scorpine showed the presence of blocking channel and cytolytic activities as well as two different structural domainsStructural and functional studies about scorpine showed the presence of blocking channel and cytolytic activities as well as two different structural domains
Structural highlights
FunctionPublication Abstract from PubMedScorpine 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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