1x5v
From Proteopedia
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| - | [[Image:1x5v.gif|left|200px]] | + | [[Image:1x5v.gif|left|200px]] |
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| - | '''NMR Structure of PcFK1''' | + | {{Structure |
| + | |PDB= 1x5v |SIZE=350|CAPTION= <scene name='initialview01'>1x5v</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR Structure of PcFK1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1X5V is a [ | + | 1X5V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Psalmopoeus_cambridgei Psalmopoeus cambridgei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X5V OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16452619 16452619] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Psalmopoeus cambridgei]] | [[Category: Psalmopoeus cambridgei]] | ||
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[[Category: inhibitory cystine knot]] | [[Category: inhibitory cystine knot]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:05:35 2008'' |
Revision as of 13:05, 20 March 2008
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NMR Structure of PcFK1
Overview
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.
About this Structure
1X5V is a Protein complex structure of sequences from Psalmopoeus cambridgei. Full crystallographic information is available from OCA.
Reference
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
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