Many gene-regulatory proteins appear to have a similar α-helical fold that binds DNA and evolved from a common precursor
- 1 March 1983
- journal article
- research article
- Published by Springer Nature in Journal of Molecular Evolution
- Vol. 19 (2), 109-114
- https://doi.org/10.1007/bf02300748
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Proposed α-helical super-secondary structure associated with protein-DNA recognitionJournal of Molecular Biology, 1982
- Homology among DNA-binding proteins suggests use of a conserved super-secondary structureNature, 1982
- Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4Journal of Molecular Biology, 1981
- Nucleotide sequence of the lexA gene of E. coliCell, 1981
- Structure at 2.3 Å resolution of the gene 5 product of bacteriophage fd: A DNA unwinding proteinJournal of Molecular Biology, 1979
- DNA sequence of the bacteriophage λ cI geneNature, 1978
- Primary structure of the λ repressorBiochemistry, 1978
- Sequence of cro gene of bacteriophage lambdaNature, 1977
- The amino acid sequence of a DNA binding protein, the gene 5 product of fd filamentous bacteriophageFEBS Letters, 1974
- An improved method of testing for evolutionary homologyJournal of Molecular Biology, 1966