Gcn4: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_2dgc| PDB=2dgc | SIZE=350| SCENE= |right|CAPTION=Gcn4 leucine zipper domain complex with DNA [[2dgc]] }} | {{STRUCTURE_2dgc| PDB=2dgc | SIZE=350| SCENE= |right|CAPTION=Gcn4 leucine zipper domain complex with DNA [[2dgc]] }} | ||
== Function == | |||
'''Gcn4''' is a yeast transcriptional activator. It belongs to a large family of eukaryotic transcription factors including Fos, Jun and CREB. | '''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 == | |||
Gcn4 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. | |||
== 3D Structures of Gcn4 == | == 3D Structures of Gcn4 == | ||
| Line 51: | Line 56: | ||
**[[1ld4]] – yGcn4 + virus coat protein + virus spike glycoprotein<br /> | **[[1ld4]] – yGcn4 + virus coat protein + virus spike glycoprotein<br /> | ||
}} | }} | ||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 12:06, 3 March 2016
Function
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 highlights
Gcn4 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.
3D Structures of Gcn4
Updated on 03-March-2016
