Homology among DNA-binding proteins suggests use of a conserved super-secondary structure
| Autor: | R. R. Yocum, Russell F. Doolittle, M. Lewis, Robert T. Sauer, Carl O. Pabo |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
DNA
Bacterial Models Molecular Protein Conformation viruses Repressor Biology DNA-binding protein Homology (biology) Viral Proteins chemistry.chemical_compound Protein structure Bacteriophages Viral Regulatory and Accessory Proteins Amino Acid Sequence Peptide sequence Protein secondary structure Genetics Multidisciplinary Biological Evolution DNA-Binding Proteins Repressor Proteins DNA binding site chemistry Nucleic Acid Conformation Carrier Proteins DNA Transcription Factors |
| Zdroj: | Nature. 298:447-451 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/298447a0 |
| Popis: | The amino acid sequences of the repressor and cro proteins of phages lambda, 434 and P22 are homologous, especially in a region in which repressor and lambda cro have a similar alpha-helix-turn-alpha-helix secondary structure. Model-building studies indicate that this structure is important in DNA binding, and we suggest it may be a common feature of many DNa-binding proteins. |
| Databáze: | OpenAIRE |
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