Summary information and primary citation
- PDB-id
-
2i13;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein-DNA
- Method
- X-ray (1.96 Å)
- Summary
- Aart, a six finger zinc finger designed to recognize
ann triplets
- Reference
-
Segal DJ, Crotty JW, Bhakta MS, Barbas CF, Horton NC
(2006): "Structure
of Aart, a Designed Six-finger Zinc Finger Peptide, Bound
to DNA." J.Mol.Biol., 363,
405-421. doi: 10.1016/j.jmb.2006.08.016.
- Abstract
- 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.
