1x5v
From Proteopedia
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| - | [[ | + | ==NMR Structure of PcFK1== |
| + | <StructureSection load='1x5v' size='340' side='right' caption='[[1x5v]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1x5v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Psalmopoeus_cambridgei Psalmopoeus cambridgei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X5V FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSL:HOMOSERINE+LACTONE'>HSL</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x5v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x5v RCSB], [http://www.ebi.ac.uk/pdbsum/1x5v PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Psalmopeotoxin I (PcFK1) is a 33-amino-acid residue peptide isolated from the venom of the tarantula Psalmopoeus cambridgei. It has been recently shown to possess strong antiplasmodial activity against the intra-erythrocyte stage of Plasmodium falciparum in vitro. Although the molecular target for PcFK1 is not yet determined, this peptide does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. We investigated the structural properties of PcFK1 to help understand the unique mechanism of action of this peptide and to enhance its utility as a lead compound for rational development of new antimalarial drugs. In this paper, we have determined the three-dimensional solution structure by (1)H two-dimensional NMR means of recombinant PcFK1, which is shown to belong to the ICK structural superfamily with structural determinants common to several neurotoxins acting as ion channels effectors. | ||
| - | + | Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum.,Pimentel C, Choi SJ, Chagot B, Guette C, Camadro JM, Darbon H Protein Sci. 2006 Mar;15(3):628-34. Epub 2006 Feb 1. PMID:16452619<ref>PMID:16452619</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Psalmopoeus cambridgei]] | [[Category: Psalmopoeus cambridgei]] | ||
[[Category: Camadro, J M.]] | [[Category: Camadro, J M.]] | ||
Revision as of 06:51, 9 June 2014
NMR Structure of PcFK1
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