Antimicrobial Peptide AP00031

     
 

APD ID:

AP00031

 
 

Name/Class:

Heliomicin (HEL-WT, defensins; insects, arthropods, invertebrates, animals; BBMm_GlcCerMOA; 3S=S; UCSS1a; Derivatives: Hel-LL)

 
 

Source:

tobacco budworm, Heliothis virescens

 
 

Sequence:

DKLIGSCVWGAVNYTSDCNGECKRRGYKGGHCGSFANVNCWCET

 
 

Length:

44

 
 

Net charge:

2

 
 

Hydrophobic residue%:

36%

 
 

Boman Index:

1.74 kcal/mol

 
 

3D Structure:

Combine Helix and Beta structure

 
 

Method:

NMR

 
 

SwissProt ID:

PDB ID: 1i2u   Go to PDB

 
 

Activity:

antifungal,

 
 

Additional info:

3 Disulphide bridges:7,32; 18,40; 22,42. Active against C. albicans and P. pastoris. Similar to plant defensin RsAFP2 (also in structure), it interacts with glucosylceramide isolated from the membranes of yeast and soybean but not humans (J Biol Chem 2004; 279: 3900-3905).Transgenic plants: expression of this peptide in tobacco improves resistance to pathogens (Montesinos E 2007 FEMS Microbiol Lett 270, 1-11). Derivatives: Based on sequence alignment with defensins from the insect family, residues K23 and R24 at the end of the helix of heliomicin were altered to leucines, leading to a gain in antibacterial activity due to the generation of an amphipathic helix. It has an identical fold to the WT with 3 disulfide bridges: 7,32; 18,40; and 22,42. You can rotate, zoom, and view the 3D structure here in the PDB . Updated 8/2010; 2/2014.

 
       
 

Title:

Solution Structures of the Antifungal Heliomicin and a Selected Variant with Both Antibacterial and Antifungal Activities.

 
 

Author:

Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F.2001

 
 

Reference:

Biochemistry 2001; 40: 11995. PubMed.

 
       

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