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2drp
From Proteopedia
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THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION
Overview
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.
About this Structure
2DRP is a Single protein structure of sequence from Drosophila melanogaster with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition., Fairall L, Schwabe JW, Chapman L, Finch JT, Rhodes D, Nature. 1993 Dec 2;366(6454):483-7. PMID:8247159
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