The BTB Domain of bric à brac Mediates Dimerization In Vitro
| Autor: | Frank A. Laski, Susan Zollman, J.-L. Couderc, Wei Chen |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Zinc finger
chemistry.chemical_classification Conserved motif Sequence alignment Cell Biology Biology biology.organism_classification Molecular biology DNA-binding protein In vitro Cell biology Amino acid chemistry Domain (ring theory) Protein folding Drosophila melanogaster Protein Dimerization Gene Molecular Biology Peptide sequence Drosophila Protein |
| Zdroj: | Molecular and Cellular Biology. 15:3424-3429 |
| ISSN: | 1098-5549 |
| DOI: | 10.1128/mcb.15.6.3424 |
| Popis: | The gene bric a 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. |
| Databáze: | OpenAIRE |
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