1l8r Citations

Structure of the retinal determination protein Dachshund reveals a DNA binding motif.

Structure 10 787-95 (2002)
Cited: 46 times
EuropePMC logo PMID: 12057194

Abstract

The Dachshund proteins are essential components of a regulatory network controlling cell fate determination. They have been implicated in eye, limb, brain, and muscle development. These proteins cannot be assigned to any recognizable structural or functional class based on amino acid sequence analysis. The 1.65 A crystal structure of the most conserved domain of human DACHSHUND is reported here. The protein forms an alpha/beta structure containing a DNA binding motif similar to that found in the winged helix/forkhead subgroup of the helix-turn-helix family. This unexpected finding alters the previously proposed molecular models for the role of Dachshund in the eye determination pathway. Furthermore, it provides a rational framework for future mechanistic analyses of the Dachshund proteins in several developmental contexts.

Articles - 1l8r mentioned but not cited (5)

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Reviews citing this publication (10)

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Articles citing this publication (31)

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  18. Ski negatively regulates erythroid differentiation through its interaction with GATA1. Ueki N, Zhang L, Hayman MJ. Mol. Cell. Biol. 24 10118-10125 (2004)
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  22. Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting. Itoh T, Fairall L, Muskett FW, Milano CP, Watson PJ, Arnaudo N, Saleh A, Millard CJ, El-Mezgueldi M, Martino F, Schwabe JW. Nucleic Acids Res. 43 2033-2044 (2015)
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  26. The SWI/SNF Subunit INI1 Contains an N-Terminal Winged Helix DNA Binding Domain that Is a Target for Mutations in Schwannomatosis. Allen MD, Freund SM, Zinzalla G, Bycroft M. Structure 23 1344-1349 (2015)
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  31. First Insights into the Subterranean Crustacean Bathynellacea Transcriptome: Transcriptionally Reduced Opsin Repertoire and Evidence of Conserved Homeostasis Regulatory Mechanisms. Kim BM, Kang S, Ahn DH, Kim JH, Ahn I, Lee CW, Cho JL, Min GS, Park H. PLoS ONE 12 e0170424 (2017)