THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEX
There is a Quite Interesting Protein Structure article for this entry.
The structure was published by Ellenberger, T.E., Brandl, C.J., Struhl, K., and Harrison, S.C., in 1992 in a paper entitled "The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 1993.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 3 biomacromolecules, namely DNA (5'-D(*TP*TP*CP*CP*TP*AP*TP*GP*AP*CP*TP*CP*AP*TP*CP*CP*A P*GP*TP*T)-3'), DNA (5'-D(*AP*AP*AP*CP*TP*GP*GP*AP*TP*GP*AP*GP*TP*CP*AP*TP*A P*GP*GP*A)-3'), and PROTEIN (GCN4).
The molecule most likely forms heterotetramers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: