The BTB Domain of bric à brac Mediates Dimerization In Vitro
Open Access
- 1 June 1995
- journal article
- retracted article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 15 (6) , 3424-3429
- https://doi.org/10.1128/mcb.15.6.3424
Abstract
The gene bric à brac (bab) is required for the proper development of the limbs and ovary in Drosophila melanogaster. bab encodes a BTB domain (also called a POZ domain), an approximately 115-amino-acid conserved motif found primarily in the N termini of zinc finger proteins. In this paper, we show that the BTB domain of bab can mediate protein dimerization in vitro. In addition, we demonstrate that the first 51 amino acids of the bab BTB domain are sufficient for dimerization, and we identify amino acids within this region that are required for binding.Keywords
This publication has 42 references indexed in Scilit:
- The POZ domain: a conserved protein-protein interaction motif.Genes & Development, 1994
- The three‐dimensional profile method using residue preference as a continuous function of residue environmentProtein Science, 1994
- TRANSLOCATION OF THE RARα LOCUS TO THE PML OR PLZF GENE IN ACUTE PROMYELOCYTIC LEUKAEMIABritish Journal of Haematology, 1994
- 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegansNature, 1994
- PLZF-RAR alpha fusion proteins generated from the variant t(11;17)(q23;q21) translocation in acute promyelocytic leukemia inhibit ligand-dependent transactivation of wild-type retinoic acid receptors.Proceedings of the National Academy of Sciences, 1994
- Nucleotide sequence of XhoI O fragment of ectromelia virus DNA reveals significant differences from vaccinia virusVirus Research, 1993
- A family of DNA virus genes that consists of fused portions of unrelated cellular genesTrends in Biochemical Sciences, 1992
- THE BACTERIAL PHOTOSYNTHETIC REACTION CENTER AS A MODEL FOR MEMBRANE PROTEINSAnnual Review of Biochemistry, 1989
- Prediction of the Secondary Structure of Proteins from their Amino Acid SequencePublished by Wiley ,1979
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978