Tom Sandbox

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1ysa.png|left|300px]]
[[Image:1ysa.png|left|300px]]
 +
==GCN4 - The Leucine Zipper==
{{STRUCTURE_2zta| PDB=2zta | SCENE= }}
{{STRUCTURE_2zta| PDB=2zta | SCENE= }}
-
===GCN4 - Leucine Zipper===
 
Blah blah information about leucine zipper GCN4.
Blah blah information about leucine zipper GCN4.
Line 10: Line 10:
{{STRUCTURE_1ysa| PDB=1ysa | SCENE= }}
{{STRUCTURE_1ysa| PDB=1ysa | SCENE= }}
-
==About this Structure==
+
===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 00:56, 9 November 2011

Contents

GCN4 - The Leucine Zipper

PDB ID 2zta

Drag the structure with the mouse to rotate
2zta, resolution 1.80Å ()
Non-Standard Residues:


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



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

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.

Proteopedia Page Contributors and Editors (what is this?)

Alan Tom

Retrieved from "http://52.214.119.220/wiki/index.php/Tom_Sandbox"
Personal tools