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spinqualitylabelsall models 2i13, resolution 1.960Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Aart, a six finger zinc finger designed to recognize ANN triplets

Overview

Cys2-His2 zinc fingers are one of the most common types of DNA-binding, domains. Modifications to zinc-finger binding specificity have recently, enabled custom DNA-binding proteins to be designed to a wide array of, target sequences. We present here a 1.96 A structure of Aart, a designed, six-zinc finger protein, bound to a consensus DNA target site. This is the, first structure of a designed protein with six fingers, and was intended, to provide insights into the unusual affinity and specificity, characteristics of this protein. Most protein-DNA contacts were found to, be consistent with expectations, while others were unanticipated or, insufficient to explain specificity. Several were unexpectedly mediated by, glycerol, water molecules or amino acid-base stacking interactions. These, results challenge some conventional concepts of recognition, particularly, the finding that triplets containing 5'A, C, or T are typically not, specified by direct interaction with the amino acid in position 6 of the, recognition helix.

About this Structure

2I13 is a Single protein structure of sequence from Mus musculus with ZN and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Aart, a designed six-finger zinc finger peptide, bound to DNA., Segal DJ, Crotty JW, Bhakta MS, Barbas CF 3rd, Horton NC, J Mol Biol. 2006 Oct 20;363(2):405-21. Epub 2006 Aug 11. PMID:16963084

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