Tom Sandbox

Blah blah information about leucine zipper GCN4.

File:2zta.png

spinqualitylabelsall models PDB ID 2zta Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2zta, resolution 1.80Å ()
Non-Standard Residues:
Structural annotation: Resources: UniProt : P03069
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

GCN4 - Leucine ZipperGCN4 - Leucine Zipper

spinqualitylabelsall models PDB ID 1ysa Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1ysa, resolution 2.90Å ()
Structural annotation: Resources: CATH : 1Ysac00, 1Ysad00 InterPro : Ipr011616, Ipr004827 Pfam : PF00170 SCOP : d1ysac_, d1ysad_ UniProt : P03069
Functional annotation: Cellular component: nucleus Biological process: positive regulation of gene-specific transcription involved in unfolded protein response amino acid biosynthetic process regulation of transcription, DNA-dependent transcription regulation of transcription from RNA polymerase II promoter Molecular function: protein dimerization activity transcription factor activity DNA binding sequence-specific DNA binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

About this StructureAbout this 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.

See AlsoSee Also

2zta 1ysa