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[[Image:1ysa.png|left|300px]]
[[Image:1ysa.png|left|300px]]
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==GCN4 - The Leucine Zipper==
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{{STRUCTURE_2zta| PDB=2zta | SCENE= }}
{{STRUCTURE_2zta| PDB=2zta | SCENE= }}
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==GCN4 - The Leucine Zipper==
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===Binding===
===Binding===
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====The Leucine Zipper====
====The Leucine Zipper====
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====Binding with DNA====
====Binding with DNA====
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===Function===
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==See Also==
==See Also==

Revision as of 00:57, 9 November 2011



PDB ID 2zta

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2zta, resolution 1.80Å ()
Non-Standard Residues:


Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Contents

GCN4 - The Leucine Zipper

Blah blah information about leucine zipper GCN4.


PDB ID 1ysa

Drag the structure with the mouse to rotate
1ysa, resolution 2.90Å ()
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



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[1].

Binding

The Leucine Zipper

Binding with DNA

Function

See Also

2zta 1ysa

Reference

  1. Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd Ed. Hoboken, NJ: Wiley, 2008.

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