1LLM

Crystal Structure of a Zif23-GCN4 Chimera Bound to DNA

Summary for 1LLM

• Entry DOI: 10.2210/pdb1llm/pdb
• Related: 1AAY 1G2D 1G2F 1YSA 1ZAA
• Descriptor: 5'-D(*TP*CP*CP*CP*AP*CP*GP*CP*GP*TP*GP*GP*G)-3', chimera of Zif23-GCN4, ZINC ION, ... (4 entities in total)
• Functional Keywords: dimerization, dna recognition, leucine zipper, structure-based design, zinc fingers, transcription-dna complex, transcription/dna
• Biological source: Mus musculus (house mouse, baker's yeast); More
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 4
• Total formula weight: 29305.33

Authors

Wolfe, S.A.,Grant, R.A.,Pabo, C.O. (deposition date: 2002-04-29, release date: 2003-09-30, Last modification date: 2024-05-22)

Primary citation

Wolfe, S.A.,Grant, R.A.,Pabo, C.O.
Structure of a designed dimeric zinc finger protein bound to DNA.
Biochemistry, 42:13401-13409, 2003

PubMed Abstract: Proteins that employ dimerization domains to bind cooperatively to DNA have a number of potential advantages over monomers with regards to gene regulation. Using a combination of structure-based design and phage display, a dimeric Cys(2)His(2) zinc finger protein has been created that binds cooperatively to DNA via an attached leucine zipper dimerization domain. This chimera, derived from components of Zif268 and GCN4, displayed excellent DNA-binding specificity, and we now report the 1.5 A resolution cocrystal structure of the Zif268-GCN4 homodimer bound to DNA. This structure shows how phage display has annealed the DNA binding and dimerization domains into a single functional unit. Moreover, this chimera provides a potential platform for the creation heterodimeric zinc finger proteins that can regulate a desired target gene through cooperative DNA recognition.

PubMed: 14621985
DOI: 10.1021/bi034830b

Experimental method

X-RAY DIFFRACTION (1.5 Å)