A code controlling specific binding of regulatory proteins to DNA
| Autor: | Alexei L. Zhuze, Vladimir G. Tumanyan, Alexander S. Zasedatelev, B.P. Gottikh, A. V. Gursky, S. L. Grokhovsky |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
chemistry.chemical_classification
Binding Sites Transcription Genetic Base pair Proteins DNA General Medicine Biology Antiparallel (biochemistry) Amino acid Models Structural DNA binding site chemistry.chemical_compound Biochemistry chemistry Genetic Code Protein Biosynthesis Genetics Nucleotide Amino Acid Sequence Molecular Biology Histidine Protein Binding Cysteine |
| Zdroj: | Molecular Biology Reports. 2:413-425 |
| ISSN: | 1573-4978 0301-4851 |
| DOI: | 10.1007/bf00366264 |
| Popis: | A possible code is suggested that describes a correspondence between amino acid sequences in stereospecific sites of regulatory proteins and nucleotide sequences at the control sites on DNA. Stereospecific sites of regulatory proteins are assumed to contain pairs of antiparallel polypeptide chain segments which form a right-hand twisted antiparallel beta-sheet with single-stranded regions at the ends of the beta-structure. The binding reaction between regulatory protein and double-helical DNA is accompanied by significant structural alterations at stereospecific sites of the protein and DNA. Half of the hydrogen bonds normally existing in beta-structure are broken upon complex formation with DNA and a new set of hydrogen bonds is formed between polypeptide amide groups and DNA base pairs. The code states a correspondence between four amino acid residues at a stereospecific site of the regulatory protein and an AT (GC) base pair at the control site. It predicts that there are six fundamental amino acid residues (serine, threonine, histidine, asparagine, glutamine and cysteine) whose arrangement in the stereospecific site determines the base pair sequence to which a given regulatory protein would bind preferentially. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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