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[[Image:1ysa.png|left|300px]] | [[Image:1ysa.png|left|300px]] | ||
==GCN4 - The Leucine Zipper== | |||
{{STRUCTURE_2zta| PDB=2zta | SCENE= }} | {{STRUCTURE_2zta| PDB=2zta | SCENE= }} | ||
Blah blah information about leucine zipper GCN4. | Blah blah information about leucine zipper GCN4. | ||
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{{STRUCTURE_1ysa| PDB=1ysa | SCENE= }} | {{STRUCTURE_1ysa| PDB=1ysa | SCENE= }} | ||
== | ===Structure=== | ||
GCN4 (PDB [[2zta]] by itself, [[1ysa]] bound to DNA) is a eukaryotic transcription factor first isolated from yeast. It is composed of two identical 52 residue alpha helix chains that grouped together to form a dimer. The dimer binds through interlocking leucine amino acids in the C terminal ends, while pinching in on the major groove of DNA in the N terminal end. The X-ray structure of the 33-residue polypeptide corresponding to the leucine zipper of GCN4 was determined by Peter Kim and Thomas Alber<ref> Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd Ed. Hoboken, NJ: Wiley, 2008. </ref>. | GCN4 (PDB [[2zta]] by itself, [[1ysa]] bound to DNA) is a eukaryotic transcription factor first isolated from yeast. It is composed of two identical 52 residue alpha helix chains that grouped together to form a dimer. The dimer binds through interlocking leucine amino acids in the C terminal ends, while pinching in on the major groove of DNA in the N terminal end. The X-ray structure of the 33-residue polypeptide corresponding to the leucine zipper of GCN4 was determined by Peter Kim and Thomas Alber<ref> Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd Ed. Hoboken, NJ: Wiley, 2008. </ref>. | ||
===Binding=== | |||
====The Leucine Zipper==== | |||
====Binding with DNA==== | |||
==See Also== | ==See Also== | ||
Revision as of 03:56, 9 November 2011
GCN4 - The Leucine ZipperGCN4 - The Leucine Zipper
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| 2zta, resolution 1.80Å () | |||||||
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| Non-Standard Residues: | |||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Blah blah information about leucine zipper GCN4.
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| 1ysa, resolution 2.90Å () | |||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
StructureStructure
GCN4 (PDB 2zta by itself, 1ysa bound to DNA) is a eukaryotic transcription factor first isolated from yeast. It is composed of two identical 52 residue alpha helix chains that grouped together to form a dimer. The dimer binds through interlocking leucine amino acids in the C terminal ends, while pinching in on the major groove of DNA in the N terminal end. The X-ray structure of the 33-residue polypeptide corresponding to the leucine zipper of GCN4 was determined by Peter Kim and Thomas Alber[1].
BindingBinding
The Leucine ZipperThe Leucine Zipper
Binding with DNABinding with DNA
See AlsoSee Also
ReferenceReference
- ↑ Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd Ed. Hoboken, NJ: Wiley, 2008.