Gcn4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
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.
 +
 +
See [[Coiled coil]].
</StructureSection>
</StructureSection>

Revision as of 11:35, 22 January 2019

Structure of Gcn4 leucine zipper domain complex with DNA (PDB entry 2dgc)

Drag the structure with the mouse to rotate

3D Structures of Gcn4

Updated on 22-January-2019

References

  1. 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Karsten Theis, Alexander Berchansky

Personal tools