1ZAA

ZINC FINGER-DNA RECOGNITION: CRYSTAL STRUCTURE OF A ZIF268-DNA COMPLEX AT 2.1 ANGSTROMS

Summary for 1ZAA

• Entry DOI: 10.2210/pdb1zaa/pdb
• Descriptor: DNA (5'-D(*AP*GP*CP*GP*TP*GP*GP*GP*CP*GP*T)-3'), DNA (5'-D(*TP*AP*CP*GP*CP*CP*CP*AP*CP*GP*C)-3'), PROTEIN (ZIF268), ... (5 entities in total)
• Functional Keywords: protein-dna complex, double helix, transcription-dna complex, transcription/dna
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus: P08046
• Total number of polymer chains: 3
• Total formula weight: 17393.66

Authors

Pavletich, N.P.,Pabo, C.O. (deposition date: 1992-09-17, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Pavletich, N.P.,Pabo, C.O.
Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A.
Science, 252:809-817, 1991

PubMed Abstract: The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap part way around the double helix. Each finger has a similar relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha helix contact the bases, and most of the contracts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.

PubMed: 2028256

Experimental method

X-RAY DIFFRACTION (2.1 Å)