scholar.google.com › citations
The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex · Authors · Affiliation.
People also ask
What protein protein interaction is the leucine zipper?
How does the leucine zipper interact with DNA?
What is the leucine zipper pattern?
What does the leucine zipper bind to?
These bZIP proteins are structurally similar and bind to DNA sequences as dimers; however, they exhibit discrete transcriptional activities, interact with ...
Jun 9, 2000 · The DNA-binding region, also known as the basic region, is found in the amino terminus and for the leucine zipper proteins, the binding segment ...
The leucine zipper is another common motif found in many DNA-binding proteins, including transcription factors such as C/EBP, Jun, Fos, GCN4, and HSF. The ...
The yeast transcriptional activator GCN4 is 1 of over 30 identified eukaryotic proteins containing the basic region leucine zipper (bZIP) DNA-binding motif.
The leucine zipper is another common motif found in many DNA-binding proteins, including transcription factors such as C/EBP, Jun, Fos, GCN4, and HSF. The ...
Missing: Complex
The localization of the leucines are critical for the DNA binding to the proteins. Leucine zippers are present in both eukaryotic and prokaryotic regulatory ...
This hypothetical structure is referred to as the "leucine zipper," and it may represent a characteristic property of a new category of DNA binding proteins.
This hypothetical structure has been proved by in vitro biochemical studies and by several crystal structural determinations that include protein–DNA complexes.
CREB bZIP-DNA complex (22) (Protein Data Bank code: 1DH3). The asymmetric unit contains one protein-DNA complex. The DNA seg- ments form a pseudo-continuous ...