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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif, where the "wings", or loops, are small β-sheets. The winged helix motif consists of two wings (W1, W2), three α-helices (H1, H2, H3) and three β-sheets (S1, S2, S3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 [ ]. The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA, while the wings make different DNA contacts, often with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.Many different proteins with diverse biological functions contain a winged helix DNA-binding domain, including transcriptional repressors such as biotin repressor, LexA repressor and the arginine repressor [ ]; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell differentiation, heat-shock transcription factor, and the general transcription factors TFIIE and TFIIF [, ]; helicases such as RuvB that promotes branch migration at the Holliday junction, and CDC6 in the pre-replication complex [, ]; endonucleases such as FokI and TnsA []; histones; and Mu transposase, where the flexible wing of the enhancer-binding domain is essential for efficient transposition []. | Name | Winged helix-like DNA-binding domain superfamily |
| Short Name | WH-like_DNA-bd_sf | Type | Homologous_superfamily |
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