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PDBsum entry 3lo6

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protein ligands metals Protein-protein interface(s) links
Antimicrobial protein PDB id
3lo6
Jmol
Contents
Protein chains
30 a.a. *
Ligands
MPD
Metals
_CL ×2
Waters ×81
* Residue conservation analysis
PDB id:
3lo6
Name: Antimicrobial protein
Title: Crystal structure of human alpha-defensin 1 (w26aba mutant)
Structure: Neutrophil defensin 1. Chain: a, b. Fragment: unp residues 65-94. Synonym: hnp-1, hp-1, hp1, defensin, alpha 1, hp 1-56, neut defensin 2, hnp-2, hp-2, hp2. Engineered: yes. Mutation: yes
Source: Synthetic: yes. Other_details: protein naturally occurs in human
Resolution:
1.56Å     R-factor:   0.170     R-free:   0.198
Authors: M.Pazgier,W.Lu
Key ref: G.Wei et al. (2010). Trp-26 imparts functional versatility to human alpha-defensin HNP1. J Biol Chem, 285, 16275-16285. PubMed id: 20220136
Date:
03-Feb-10     Release date:   09-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P59665  (DEF1_HUMAN) -  Neutrophil defensin 1
Seq:
Struc:
94 a.a.
30 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
J Biol Chem 285:16275-16285 (2010)
PubMed id: 20220136  
 
 
Trp-26 imparts functional versatility to human alpha-defensin HNP1.
G.Wei, M.Pazgier, E.de Leeuw, M.Rajabi, J.Li, G.Zou, G.Jung, W.Yuan, W.Y.Lu, R.I.Lehrer, W.Lu.
 
  ABSTRACT  
 
We performed a comprehensive alanine scan of human alpha-defensin HNP1 and tested the ability of the resulting analogs to kill Staphylococcus aureus, inhibit anthrax lethal factor, and bind human immunodeficiency virus-1 gp120. By far, the most deleterious mutation for all of these functions was W26A. The activities lost by W26A-HNP1 were restored progressively by replacing W26 with non-coded, straight-chain aliphatic amino acids of increasing chain length. The hydrophobicity of residue 26 also correlated with the ability of the analogs to bind immobilized wild type HNP1 and to undergo further self-association. Thus, the hydrophobicity of residue 26 is not only a key determinant of the direct interactions of HNP1 with target molecules, but it also governs the ability of this peptide to form dimers and more complex quaternary structures at micromolar concentrations. Although all defensin peptides are cationic, their amphipathicity is at least as important as their positive charge in enabling them to participate in innate host defense.