Gcn4: Difference between revisions
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== Function == | == Function == | ||
'''Gcn4''' is a yeast transcriptional activator. It belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. <ref>PMID:7934812</ref> Gcn4-pLI is a 33-residue peptide of the dimerization domain of Gcn4. See also [[Intrinsically Disordered Protein]]. | '''Gcn4''' or '''General control protein Gcn4''' is a yeast transcriptional activator. It belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. <ref>PMID:7934812</ref> Gcn4-pLI is a 33-residue peptide of the dimerization domain of Gcn4. See also [[Intrinsically Disordered Protein]]. | ||
== Structural highlights == | == Structural highlights == | ||
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== 3D Structures of Gcn4 == | == 3D Structures of Gcn4 == | ||
[[ | [[Gcn4 3D Structures]] | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 11:32, 12 March 2023
FunctionGcn4 or General control protein Gcn4 is a yeast transcriptional activator. It belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. [1] Gcn4-pLI is a 33-residue peptide of the dimerization domain of Gcn4. See also Intrinsically Disordered Protein. Structural highlightsGcn4 and other family members have a DNA recognition motif consisting of a coiled-coil dimerization element, the leucine-zipper, and an adjoining basic region, which mediates DNA binding. This basic region is largely unstructured in the absence of DNA, addition of DNA containing a Gcn4 binding site induces the transition of this region from unstructured to α-helical. See Coiled coil. 3D Structures of Gcn4
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