General Information
-
DRAMP ID
- DRAMP02698
-
Peptide Name
- Rhesus macaque oral alpha-defensins (ROADs; primates, mammals, animals)
-
Source
- Macaca mulatta (Rhesus monkey)
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Family
- Belongs to the alpha-defensin family
-
Gene
- Not found
-
Sequence
- RRTCHCRSRCLRRESNSGSCNINGRIFSLCCR
-
Sequence Length
- 32
-
UniProt Entry
- B5AKV3
-
Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal
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Target Organism
-
- Gram-positive bacterium: Staphylococcus aureus;
- Gram-negative bacterium: Escherichia coli.
- Fungi: Candida albicans.
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
-
Cytotoxicity
- No cytotoxicity information found in the reference(s) presented
-
Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Cyclic
-
N-terminal Modification
- Free
-
C-terminal Modification
- Free
-
Nonterminal Modifications and Unusual Amino Acids
- Disulfide bonds between Cys4 and Cys31; Cys6 and Cys20; Cys10 and Cys30.
-
Stereochemistry
- L
-
Structure
- Beta strand (3 strands; 19 residues)
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Structure Description
- NMR spectroscopy shows that Synthetic ROAD-1 adopts the canonical disulfide pairing and alpha-defensin fold.
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Helical Wheel Diagram
-
PDB ID
- 2K1I resolved by NMR.
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Predicted Structure
- There is no predicted structure for DRAMP02698.
Physicochemical Information
-
Formula
- C145H251N61O44S6
Absent Amino Acids
- ADKMPQVWY
Common Amino Acids
- R
Mass
- 3745.33
PI
- 10.44
Basic Residues
- 9
Acidic Residues
- 1
Hydrophobic Residues
- 5
Net Charge
- +8
-
Boman Index
- -138.1
Hydrophobicity
- -0.759
Aliphatic Index
- 48.75
Half Life
-
- Mammalian:1 hour
- Yeast:2 min
- E.coli:2 min
Extinction Coefficient Cystines
- 375
Absorbance 280nm
- 12.1
Polar Residues
- 17
DRAMP02698
![DRAMP02698 chydropathy plot](http://dramp.cpu-bioinfor.org/tmp/all_info_png/pepwindow_DRAMP02698.1.png)
Comments Information
Function
- ROAD-1 is active against Staphylococcus aureus, Escherichia coli, and Candida albicans in a concentration-dependent manner. The antimicrobial mechanism of defensins has been correlated with their ability to disrupt and permeabilize the cell envelope, activities that depend on the surface features of the folded peptide.
PTM
- Contains three disulfide bonds.
Literature Information
- ·Literature 1
-
Title
- Synthesis, structure, and activities of an oral mucosal alpha-defensin from rhesus macaque.
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Pubmed ID
- 18930922
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Reference
- J Biol Chem. 2008 Dec 19;283(51):35869-35877.
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Author
- Vasudevan S, Yuan J, Osapay G, Tran P, Tai K, Liang W, Kumar V, Selsted ME, Cocco MJ.