9vcd | pdb_00009vcd

N-terminal dimeric C2H2-domain of Drosophila melanogaster IMZF protein

spinqualitylabelsall models 9vcd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9vcd is a 2 chain structure with sequence from Drosophila melanogaster. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, models Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed C2H2 proteins, characterized by DNA-binding C2H2-type zinc finger domains, constitute the largest group of transcription factors. In addition to binding DNA, C2H2 domains can mediate protein-protein interactions, facilitating the oligomerization of C2H2 proteins. In this study, we identified eight C2H2 proteins in the Drosophila genome that feature a unique single C2H2 domain containing a conserved "CGxPhi" motif. Yeast two-hybrid assays, size-exclusion chromatography coupled with multi-angle light scattering, and chemical cross-linking experiments revealed a strong propensity of these domains to form dimers. Using NMR spectroscopy, we determined the solution structure of the dimeric C2H2 domain from the IMZF (Immune-mediated Zinc Finger) protein, providing structural evidence for the dimerization of C2H2 domains. Dimerization is mediated by the interface between the core C2H2 fold and the adjacent beta-strand containing the CGxPhi motif, which was further validated by structure-guided mutagenesis. A bioinformatic survey showed that "CGxPhi"-type C2H2 domains are specific to Diptera. Finally, our predictions demonstrate that dimerizing C2H2 domains containing additional structural elements could be widespread among eukaryotic taxa, with the highest prevalence in insects. These findings establish that single C2H2 domains can mediate self-association and identify the CGxPhi-type C2H2 domains as a distinct structural subclass specific to dipteran insects. Beyond DNA binding: single C2H2 zinc fingers with adjacent beta-strands mediate dimerization in Drosophila transcription factors.,Balagurov KI, Mariasina SS, Dukhalin SD, Sluchanko NN, Golovnina AA, Khrustaleva AM, Maksimenko OG, Arkova OV, Stepanenko AA, Bocharov EV, Polshakov VI, Georgiev PG, Bonchuk AN Nucleic Acids Res. 2026 Jan 5;54(1):gkaf1425. doi: 10.1093/nar/gkaf1425. PMID:41495890 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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