Gcn4
From Proteopedia
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| - | {{STRUCTURE_2dgc| PDB=2dgc | SIZE=350| SCENE= |right|CAPTION=Gcn4 complex with DNA [[2dgc]] }} | + | {{STRUCTURE_2dgc| PDB=2dgc | SIZE=350| SCENE= |right|CAPTION=Gcn4 leucine zipper domain complex with DNA [[2dgc]] }} |
'''Gcn4''' is a yeast transcriptional activator. It belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. All 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. Gcn4-pLI is a 33-residue peptide of the dimerization domain of Gcn4. See also [[Intrinsically Disordered Protein]]. | '''Gcn4''' is a yeast transcriptional activator. It belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. All 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. Gcn4-pLI is a 33-residue peptide of the dimerization domain of Gcn4. See also [[Intrinsically Disordered Protein]]. | ||
Revision as of 11:56, 3 March 2016
Gcn4 is a yeast transcriptional activator. It belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. All 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. Gcn4-pLI is a 33-residue peptide of the dimerization domain of Gcn4. See also Intrinsically Disordered Protein.
3D Structures of Gcn4
Updated on 03-March-2016
