1f2i: Difference between revisions

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[[Image:1f2i.~~gif~~|left|200px]]

[[Image:1f2i.png|left|200px]]

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~~'''~~COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA~~'''~~

===COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11427887}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11427887 is the PubMed ID number.

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==About this Structure==

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[[Category: Protein-dna complex]]

[[Category: Zinc finger]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:48:46 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:23:45 2008''

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-[[Image:1f2i.gif|left|200px]]
+{{Seed}}
+[[Image:1f2i.png|left|200px]]
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 {{STRUCTURE_1f2i|  PDB=1f2i  |  SCENE=  }}
-'''COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11427887}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11427887 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11427887}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Protein-dna complex]]
 [[Category: Zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:48:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:23:45 2008''