General Information
-
DRAMP ID
- DRAMP00298
-
Peptide Name
- U1-theraphotoxin-Pc1a (U2-TRTX-Pc1a; Psalmopeotoxin-2; PcFK2; Plants)
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Source
- Psalmopoeus cambridgei (Trinidad chevron tarantula)
-
Family
- Not found
-
Gene
- Not found
-
Sequence
- RCLPAGKTCVRGPMRVPCCGSCSQNKCT
-
Sequence Length
- 28
-
UniProt Entry
- P0C202
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antiplasmodial, Cytotoxic
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Target Organism
- Plasmodium falciparum (IC50=1.15 µM).
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
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N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
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Nonterminal Modifications and Unusual Amino Acids
- Not included yet
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Stereochemistry
- Not included yet
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Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP00298.
Physicochemical Information
-
Formula
- C116H203N41O35S7
Absent Amino Acids
- DEFHIWY
Common Amino Acids
- C
Mass
- 2956.56
PI
- 9.22
Basic Residues
- 5
Acidic Residues
- 0
Hydrophobic Residues
- 4
Net Charge
- +5
-
Boman Index
- -52.32
Hydrophobicity
- -0.229
Aliphatic Index
- 38.21
Half Life
-
- Mammalian:1 hour
- Yeast:2 min
- E.coli:2 min
Extinction Coefficient Cystines
- 375
Absorbance 280nm
- 13.89
Polar Residues
- 14
DRAMP00298
Comments Information
Function
- Possess strong antiplasmodial activity against the intra-erythrocyte stage of P.falciparum in vitro. Specifically interacts with infected erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. Has neither antibacterial nor antifungal activity.
Tissue specificity
- Expressed by the venom gland.
Domain
- The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin By similarity.
Miscellaneous
- Usually endopeptidases cleave the propeptide at the C-terminus of the basic doublet (Arg-37-38-Arg), but here, it seems that the endopeptidase cleaves the precursor within the doublet.
PTM
- Contains three disulfide bonds (By similarity).
Literature Information
- ·Literature 1
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Title
- Isolation and characterization of Psalmopeotoxin I and II: two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei.
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Pubmed ID
- 15304333
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Reference
- FEBS Lett. 2004 Aug 13;572(1-3):109-117.
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Author
- Choi SJ, Parent R, Guillaume C, Deregnaucourt C, Delarbre C, Ojcius DM, Montagne JJ, C©l©rier ML, Phelipot A, Amiche M, Molgo J, Camadro JM, Guette C.