Gcn4
From Proteopedia
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| + | <StructureSection load='2dgc' size='350' side='right' caption='Structure of Gcn4 leucine zipper domain complex with DNA (PDB entry [[2dgc]])' scene=''> | ||
== Function == | == Function == | ||
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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. | 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. | ||
| + | </StructureSection> | ||
== 3D Structures of Gcn4 == | == 3D Structures of Gcn4 == | ||
Revision as of 08:18, 24 May 2017
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3D Structures of Gcn4
Updated on 24-May-2017
References
- ↑ Hinnebusch AG. Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol Microbiol. 1993 Oct;10(2):215-23. PMID:7934812
