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Solution structure of drosomycin, the first inducible antifungal protein from insects
Author(s) -
Landon Céline,
Sodano Patrick,
Hetru Charles,
Hoffmann Jules,
Ptak Marius
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060908
Subject(s) - antifungal , cysteine , drosophila melanogaster , structural motif , defensin , biology , biochemistry , disulfide bond , scorpion , peptide sequence , amino acid , protein structure , protein tertiary structure , peptide , chemistry , stereochemistry , microbiology and biotechnology , venom , gene , enzyme
Drosomycin is the first antifungal protein characterized recently among the broad family of inducible peptides and proteins produced by insects to respond to bacterial or septic injuries. It is a small protein of 44 amino acid residues extracted from Drosophila melanogaster that exhibits a potent activity against filamentous fungi. Its three‐dimensional structure in aqueous solution was determined using 1 H 2D NMR. This structure, involving an α‐helix and a twisted three‐stranded β‐sheet, is stabilized by three disulfide bridges. The corresponding Cysteine Stabilized αβ (CSαβ) motif, which was found in other defense proteins such as the antibacterial insect defensin A, short‐ and long‐chain scorpion toxins, as well as in plant thionins and potent antifungal plant defensins, appears as remarkably persistent along evolution.