1f2i
From Proteopedia
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| - | [[Image:1f2i.gif|left|200px]] | + | [[Image:1f2i.gif|left|200px]] |
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| - | '''COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA''' | + | {{Structure |
| + | |PDB= 1f2i |SIZE=350|CAPTION= <scene name='initialview01'>1f2i</scene>, resolution 2.35Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= GENE FOR ZIF12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F2I is a [ | + | 1F2I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2I OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11427887 11427887] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:29 2008'' |
Revision as of 09:03, 20 March 2008
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| , resolution 2.35Å | |||||||
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| Ligands: | |||||||
| Gene: | GENE FOR ZIF12 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA
Overview
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 Structure
1F2I is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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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