{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,15]],"date-time":"2025-12-15T13:31:27Z","timestamp":1765805487019},"reference-count":28,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2002,2,28]],"date-time":"2002-02-28T00:00:00Z","timestamp":1014854400000},"content-version":"vor","delay-in-days":515,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Peptide Research"],"published-print":{"date-parts":[[2000,10]]},"abstract":"<jats:p><jats:bold>Abstract:<\/jats:bold> Drosomycin is the first strictly antifungal protein isolated from an insect (<jats:italic>Drosophila melanogaster<\/jats:italic>). The solution structure of this 44\u2010residue protein has been reported previously. It involves a three\u2010stranded \u03b2\u2010sheet and an \u03b1\u2010helix, the protein global fold being maintained by four disulfide bridges. <jats:italic>Rs<\/jats:italic>\u2010AFP2 is a plant antifungal protein exhibiting 41% sequence similarity with drosomycin. Mutational analysis of <jats:italic>Rs<\/jats:italic>\u2010AFP2 showed the importance of some residues in the antifungal activity of the protein against the fungus target. In order to determine the structural features responsible for antifungal activity in both drosomycin and <jats:italic>Rs<\/jats:italic>\u2010AFP2, we modeled the three\u2010dimensional structure of <jats:italic>Rs<\/jats:italic>\u2010AFP2, and of other antifungal proteins, using the solution structure of drosomycin as a template. Structure analysis of drosomycin and <jats:italic>Rs<\/jats:italic>\u2010AFP2, and comparisons with the other modeled antifungal structures, revealed that the two proteins shared a hydrophobic cluster located at the protein surface in which a lysine residue is embedded. Based on these close structural similarities and the experimental data available for <jats:italic>Rs<\/jats:italic>\u2010AFP2 mutants, an antifungal active site of the insect protein is proposed.<\/jats:p>","DOI":"10.1034\/j.1399-3011.2000.00757.x","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T07:45:52Z","timestamp":1027669552000},"page":"231-238","source":"Crossref","is-referenced-by-count":25,"title":["The active site of drosomycin, a small insect antifungal protein, delineated by comparison with the modeled structure of <i>Rs<\/i>\u2010AFP2, a plant antifungal protein"],"prefix":"10.1111","volume":"56","author":[{"given":"C.","family":"Landon","sequence":"first","affiliation":[]},{"given":"F.","family":"Vovelle","sequence":"additional","affiliation":[]},{"given":"P.","family":"Sodano","sequence":"additional","affiliation":[]},{"given":"A.","family":"Pajon","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2008,12,5]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0952-7915(96)80098-7"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(20)30111-3"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560060908"},{"key":"e_1_2_6_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(01)00177-0"},{"key":"e_1_2_6_6_2","first-page":"573","article-title":"Small cysteine\u2010rich antifungal proteins from radish: their role in host defense","volume":"7","author":"Terras F.R.G.","year":"1995","journal-title":"Plant Cell"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1104\/pp.108.4.1353"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(95)00666-w"},{"key":"e_1_2_6_9_2","first-page":"51","article-title":"Solution conformation of Raphanus sativus antifungal protein 1 (Rs\u2010AFP1) by 1H nuclear magnetic resonance. 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