Solution structure of the basic region from the transcriptional activator GCN4
| Autor: | H. Gausepohl, H. S. Pasley, Toby J. Gibson, A. Pastore, Vladimir Saudek, Rainer Frank |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Circular dichroism
Leucine zipper Magnetic Resonance Spectroscopy Saccharomyces cerevisiae Proteins Stereochemistry Protein Conformation Molecular Sequence Data Peptide Biochemistry Fungal Proteins chemistry.chemical_compound Transcription (biology) Amino Acid Sequence Isoelectric Point Transcriptional Activator chemistry.chemical_classification Circular Dichroism bZIP domain Hydrogen Bonding DNA-Binding Proteins Solutions chemistry Nucleic acid Peptides Protein Kinases DNA Transcription Factors |
| Zdroj: | Biochemistry. 30(5) |
| ISSN: | 0006-2960 |
| Popis: | The structure of the basic region (i.e., the region responsible for sequence-specific binding to DNA) of the transcriptional activator GCN4 was studied. Two peptide fragments containing either the basic region alone (residues 240-280) or the basic and the dimerization leucine zipper domains (220-280) were synthesized and investigated by nuclear magnetic resonance and circular dichroic spectroscopy. The basic region in the absence of DNA appears as a mobile flexible segment folded into a loose helix. The helical stability increases upon addition of trifluoroethanol and/or lowering of the temperature. Dimerization via the leucine zipper does not affect the three-dimensional structure of the basic region. Possible consequences for the binding to DNA are discussed. |
| Databáze: | OpenAIRE |
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