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PDBsum entry 3h6c
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Antimicrobial protein
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PDB id
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3h6c
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References listed in PDB file
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Key reference
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Title
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Trp-26 imparts functional versatility to human alpha-Defensin hnp1.
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Authors
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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.
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Ref.
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J Biol Chem, 2010,
285,
16275-16285.
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PubMed id
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Abstract
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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.
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