1myn
SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURESSOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURES
Structural highlights
FunctionDMYC_DROME Possesses antifungal activity and is active against a relatively broad spectrum of filamentous fungi. It inhibits spore germination at high concentrations and at low concentrations delays growth of hyphae which subsequently exhibit abnormal morphology. Spz C-106 in the hemolymph controls expression of the antifungal peptide by acting as a ligand of Tl and inducing an intracellular signaling pathway.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDrosomycin 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 1H 2D NMR. This structure, involving an alpha-helix and a twisted three-stranded beta-sheet, is stabilized by three disulfide bridges. The corresponding Cysteine Stabilized alpha beta (CS alpha beta) 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. Solution structure of drosomycin, the first inducible antifungal protein from insects.,Landon C, Sodano P, Hetru C, Hoffmann J, Ptak M Protein Sci. 1997 Sep;6(9):1878-84. PMID:9300487[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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