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1myn

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Revision as of 06:56, 25 August 2021

SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURES

Structural highlights

1myn is a 1 chain structure with sequence from Drome. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DMYC_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 PubMed

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 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

↑ Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell. 1996 Sep 20;86(6):973-83. PMID:8808632
↑ Weber AN, Tauszig-Delamasure S, Hoffmann JA, Lelievre E, Gascan H, Ray KP, Morse MA, Imler JL, Gay NJ. Binding of the Drosophila cytokine Spatzle to Toll is direct and establishes signaling. Nat Immunol. 2003 Aug;4(8):794-800. Epub 2003 Jul 20. PMID:12872120 doi:http://dx.doi.org/10.1038/ni955
↑ Landon C, Sodano P, Hetru C, Hoffmann J, Ptak M. Solution structure of drosomycin, the first inducible antifungal protein from insects. Protein Sci. 1997 Sep;6(9):1878-84. PMID:9300487

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1myn"

@@ Line 3: / Line 3: @@
 <StructureSection load='1myn' size='340' side='right'caption='[[1myn]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1myn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MYN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1myn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYN FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1myn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myn OCA], [http://pdbe.org/1myn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1myn RCSB], [http://www.ebi.ac.uk/pdbsum/1myn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1myn ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1myn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myn OCA], [https://pdbe.org/1myn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1myn RCSB], [https://www.ebi.ac.uk/pdbsum/1myn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1myn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DMYC_DROME DMYC_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.<ref>PMID:8808632</ref> <ref>PMID:12872120</ref>
+[[https://www.uniprot.org/uniprot/DMYC_DROME DMYC_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.<ref>PMID:8808632</ref> <ref>PMID:12872120</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1myn

From Proteopedia

Revision as of 06:56, 25 August 2021

SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL PROTEIN FROM INSECTS, NMR, 15 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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