Affolter et al., 1990, Proc. Natl. Acad. Sci. U.S.A. 87: 4093--4097

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Affolter et al., 1990, Proc. Natl. Acad. Sci. U.S.A. 87: 4093--4097
FlyBase Identifier FBrf0052840
FlyBase URL http://flybase.org/reports/FBrf0052840.html
Publication Type paper
Publication Year 1990
PubMed ID 1971945
PubMed URL http://www.ncbi.nlm.nih.gov/pubmed/1971945

Title

DNA binding properties of the purified Antennapedia homeodomain.

Abstract

The in vitro DNA binding properties of a purified 68-amino acid Antennapedia homeodomain (Antp HD) peptide have been analyzed. Equilibrium and kinetic binding studies showed that stable DNA-protein complexes are formed with a Kd of 1.6 x 10(-9) M and 1.8 x 10(-10) M, respectively. Heterodimer analysis led to the conclusion that Antp HD interacts in vitro as a monomer with the DNA target sites used in our study. The results of methylation and ethylation interference studies indicated that the Antp HD closely approaches the target DNA primarily from one side in a region extending across three phosphate backbones. The DNA binding properties of the Antp HD and prokaryotic DNA binding domains that share a helix-turn-helix motif are compared.

Genes from Reference

Gene(s) Dmel\Antp
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