2drp: Difference between revisions

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[[Image:2drp.gif|left|200px]]
{{Seed}}
[[Image:2drp.png|left|200px]]


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{{STRUCTURE_2drp|  PDB=2drp  |  SCENE=  }}  
{{STRUCTURE_2drp|  PDB=2drp  |  SCENE=  }}  


'''THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION'''
===THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION===




==Overview==
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The Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition suggesting that the zinc-finger might represent a candidate template for designing proteins to recognize DNA. Residues at three key positions in an alpha-helical 'reading head' play a dominant role in base-recognition and have been targets for mutagenesis experiments aimed at deriving a recognition code. Here we report the structure of a two zinc-finger DNA-binding domain from the protein Tramtrack complexed with DNA. The amino-terminal zinc-finger and its interaction with DNA illustrate several novel features. These include the use of a serine residue, which is semi-conserved and located outside the three key positions, to make a base contact. Its role in base-recognition correlates with a large, local, protein-induced deformation of the DNA helix at a flexible A-T-A sequence and may give insight into previous mutagenesis experiments. It is apparent from this structure that zinc-finger/DNA recognition is more complex than was originally perceived.
The line below this paragraph, {{ABSTRACT_PUBMED_8247159}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8247159 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8247159}}


==About this Structure==
==About this Structure==
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[[Category: Double helix]]
[[Category: Double helix]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
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