Antimicrobial Peptide AP00628“>006282183.33 %100.0 %AVP
     
 

APD ID:

AP00628

 
 

Name/Class:

LL-23 (LL23, derived from its parent cathelicidin; UCLL1; humans; primates, mammals, animals)

 
 

Source:

human skin, Homo sapiens

 
 

Sequence:

LLGDFFRKSKEKIGKEFKRIVQR

 
 

Length:

23

 
 

Net charge:

5

 
 

Hydrophobic residue%:

34%

 
 

Boman Index:

3.01 kcal/mol

 
 

3D Structure:

Helix

 
 

Method:

NMR

 
 

SwissProt ID:

PDB ID: 2LMF   Go to PDB

 
 

Activity:

Anti-Gram+ & Gram-, Antifungal,

 
 

Crucial residues:

 
 

Additional info:

A natural innate peptide corresponding to the N-terminal 23 residues of human LL-37. Its structure and dynamics have been characterized in membrane-mimetic models (SDS, DPC, and D8PG) using both unlabeled and 15N-labeled samples (Biochemistry 2012). You can rotate, zoom, and view the 3D structure bound to SDS micelleshere in the PDB . The Ser9 site splits the hydrophobic surface of the amphipathic helix into two domains, which explains its poor antimicrobial activity (active against only susceptible bacterial strains). Based on the 3D structure, however, a mutation of Ser9 with either Ala or Val modulates the activities of LL-23. The Ser9Val mutant can better penetrate into membranes, leading to improved antibacterial activity. APD update July 10/2012; 12/10/12 GW.

 
       
 

Title:

Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin

 
 

Author:

Yamasaki K, Schauber J, Coda A, Lin H, Dorschner RA, Schechter NM, Bonnart C, Descargues P, Hovnanian A, Gallo RL.2006

 
 

Reference:

FASEB J. 2006 Oct;20(12):2068-80.PubMed.

 
       

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