3H6C

Crystal structure of human alpha-defensin 1 (Mutant Gln22Ala)

3H6C の概要

• エントリーDOI: 10.2210/pdb3h6c/pdb
• 関連するPDBエントリー: 3GNY 3GO0
• 分子名称: Neutrophil defensin 1, DI(HYDROXYETHYL)ETHER, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: antimicrobial peptide, q22a mutant of human alpha defensin 1 q22a mutant of human neutrophil peptide 1, hnp1(q22a), antibiotic, antimicrobial, antiviral defense, defensin, disulfide bond, fungicide, phosphoprotein, secreted, antimicrobial protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P59665
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7108.72

構造登録者

Pazgier, M.,Lu, W. (登録日: 2009-04-23, 公開日: 2010-03-09, 最終更新日: 2024-11-20)

主引用文献

Wei, G.,Pazgier, M.,de Leeuw, E.,Rajabi, M.,Li, J.,Zou, G.,Jung, G.,Yuan, W.,Lu, W.Y.,Lehrer, R.I.,Lu, W.
Trp-26 imparts functional versatility to human alpha-defensin HNP1.
J.Biol.Chem., 285:16275-16285, 2010

PubMed 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.

PubMed: 20220136
DOI: 10.1074/jbc.M110.102749

実験手法

X-RAY DIFFRACTION (1.63 Å)