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

Seung Sup Kim, Rong Guang Zhang, Steve E. Braunstein, Andrzej Joachimiak, Ales Cvekl, Rashmi S. Hegde

Research output: Contribution to journalArticle

58 Scopus citations

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 Å crystal structure of the most conserved domain of human DACHSHUND is reported here. The protein forms an α/β 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.

Original languageEnglish (US)
Pages (from-to)787-795
Number of pages9
JournalStructure
Volume10
Issue number6
DOIs
StatePublished - Jun 24 2002

Keywords

  • Crystal structure
  • DNA binding
  • Dachshund
  • Development
  • Eye
  • Winged helix

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Kim, S. S., Zhang, R. G., Braunstein, S. E., Joachimiak, A., Cvekl, A., & Hegde, R. S. (2002). Structure of the retinal determination protein Dachshund reveals a DNA binding motif. Structure, 10(6), 787-795. https://doi.org/10.1016/S0969-2126(02)00769-4