Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Structure of the specificity domain of the Dorsal homologue Gambif1 bound to DNA


Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

(Publisher version), 2MB

Supplementary Material (public)
There is no public supplementary material available

Cramer, P., Varrot, A., Barillas-Mury, C., Kafatos, F. C., & Müller, C. W. (1999). Structure of the specificity domain of the Dorsal homologue Gambif1 bound to DNA. Structure, 7(7), 841-852. doi:10.1016/S0969-2126(99)80107-5.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-871E-9
Background: NF-κB/Rel transcription factors play important roles in immunity and development in mammals and insects. Their activity is regulated by their cellular localization, homo- and heterodimerization and association with other factors on their target gene promoters. Gambif1 fromAnopheles gambiae is a member of the Rel family and a close homologue of the morphogen Dorsal, which establishes dorsoventral polarity in theDrosophila embryo.Results: We present the crystal structure of the N-terminal specificity domain of Gambif1 bound to DNA. This first structure of an insect Rel protein–DNA complex shows that Gambif1 binds a GGG half-site element using a stack of three arginine sidechains. Differences in affinity to Dorsal binding sites in target gene promoters are predicted to arise from base changes in these GGG elements. An arginine that is conserved in class II Rel proteins (members of which contain a transcription activation domain) contacts the outermost guanines of the DNA site. This previously unseen specific contact contributes strongly to the DNA-binding affinity and might be responsible for differences in specificity between Rel proteins of class I and II.Conclusions: The Gambif1–DNA complex structure illustrates how differences in Dorsal affinity to binding sites in developmental gene promoters are achieved. Comparison with other Rel–DNA complex structures leads to a general model for DNA recognition by Rel proteins.