1f2i
COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA
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| , resolution 2.35Å | |||||||
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| Ligands: | |||||||
| Gene: | GENE FOR ZIF12 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Protein-protein interactions often play a crucial role in stabilizing protein-DNA complexes and thus facilitate site-specific DNA recognition. We have worked to incorporate such protein-protein contacts into our design and selection strategies for short peptide extensions that promote cooperative binding of zinc finger proteins to DNA. We have determined the crystal structure of one of these fusion protein-DNA complexes. The selected peptide extension was found to mediate dimerization by reaching across the dyad axis and contacting a hydrophobic patch on the surface of the zinc finger bound to the adjacent DNA site. The peptide-zinc finger protein interactions observed in this structure are similar to those of some homeodomain heterodimers. We also find that the region of the zinc finger surface contacted by the selected peptide extension corresponds to surfaces that also make key interactions in the zinc finger proteins GLI and SWI5.
About this StructureAbout this Structure
1F2I is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Selected peptide extension contacts hydrophobic patch on neighboring zinc finger and mediates dimerization on DNA., Wang BS, Grant RA, Pabo CO, Nat Struct Biol. 2001 Jul;8(7):589-93. PMID:11427887
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