Crystal structure of Diedel, a marker of the immune response of Drosophila melanogaster
| Autor: | Charles Hetru, Christine Kellenberger, Alain Roussel, Franck Coste, Vanessa Bobezeau, Cordula Kemp, Jean-Luc Imler |
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| Přispěvatelé: | Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Réponse immunitaire et developpement chez les insectes (RIDI - UPR 9002), Université de Strasbourg (UNISTRA)-Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2011 |
| Předmět: |
MESH: Signal Transduction
Protein Folding lcsh:Medicine Crystallography X-Ray Biochemistry MESH: Protein Structure Tertiary Protein structure Molecular Cell Biology Melanogaster MESH: Janus Kinases Pathology Drosophila Proteins MESH: Animals lcsh:Science Genetics 0303 health sciences Multidisciplinary biology Schneider 2 cells 030302 biochemistry & molecular biology MESH: Transcription Factors Animal Models Cell biology STAT Transcription Factors Drosophila melanogaster Medicine MESH: Aphids Drosophila Protein Signal Transduction Research Article Signal peptide MESH: Drosophila Proteins MESH: Protein Folding Immunology Sequence alignment MESH: Drosophila melanogaster Molecular Genetics 03 medical and health sciences Model Organisms Diagnostic Medicine Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Binding site Biology 030304 developmental biology Janus Kinases lcsh:R Immunity Proteins MESH: STAT Transcription Factors biology.organism_classification MESH: Crystallography X-Ray Protein Structure Tertiary Aphids lcsh:Q Clinical Immunology Transcription Factors General Pathology |
| Zdroj: | PLoS ONE PLoS ONE, Public Library of Science, 2012, 7 (3), pp.e33416. ⟨10.1371/journal.pone.0033416⟩ PLoS ONE, Vol 7, Iss 3, p e33416 (2012) |
| ISSN: | 1932-6203 |
| DOI: | 10.1371/journal.pone.0033416⟩ |
| Popis: | International audience; BACKGROUND: The Drosophila melanogaster gene CG11501 is up regulated after a septic injury and was proposed to act as a negative regulator of the JAK/STAT signaling pathway. Diedel, the CG11501 gene product, is a small protein of 115 residues with 10 cysteines. METHODOLOGY/PRINCIPAL FINDINGS: We have produced Diedel in Drosophila S2 cells as an extra cellular protein thanks to its own signal peptide and solved its crystal structure at 1.15 Å resolution by SIRAS using an iodo derivative. Diedel is composed of two sub domains SD1 and SD2. SD1 is made of an antiparallel β-sheet covered by an α-helix and displays a ferredoxin-like fold. SD2 reveals a new protein fold made of loops connected by four disulfide bridges. Further structural analysis identified conserved hydrophobic residues on the surface of Diedel that may constitute a potential binding site. The existence of two conformations, cis and trans, for the proline 52 may be of interest as prolyl peptidyl isomerisation has been shown to play a role in several physiological mechanisms. The genome of D. melanogaster contains two other genes coding for proteins homologous to Diedel, namely CG43228 and CG34329. Strikingly, apart from Drosophila and the pea aphid Acyrthosiphon pisum, Diedel-related sequences were exclusively identified in a few insect DNA viruses of the Baculoviridae and Ascoviridae families. CONCLUSION/SIGNIFICANCE: Diedel, a marker of the Drosophila antimicrobial/antiviral response, is a member of a small family of proteins present in drosophilids, aphids and DNA viruses infecting lepidopterans. Diedel is an extracellular protein composed of two sub-domains. Two special structural features (hydrophobic surface patch and cis/trans conformation for proline 52) may indicate a putative interaction site, and support an extra cellular signaling function for Diedel, which is in accordance with its proposed role as negative regulator of the JAK/STAT signaling pathway. |
| Databáze: | OpenAIRE |
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