Sequence-specific DNA recognition by Cys{sub 2}, His{sub 2} zinc fingers
- Univ. of Washington, Seattle, WA (United States)
Structural and mutagenesis studies on a variety of zine finger domains have revealed a general scheme by which these motifs perform sequence-specific DNA recognition. As is the4 case for many other types of DNA binding motifs, the side chains responsible for sequence-specific interactions with DNA bases emanate from an {alpha}-helix. Thus, the small motifs can be thought of as protein scaffolds that stabilize and present the helical structure onto which specific DNA binding activities are placed. Unlike the majority of characterized DNA binding motifs, zinc finger proteins do not bind to DNA as dimers and therefore could potentially recognize any specific sequence of DNA, including nonpalidromic sequences. These properties suggest that the Cys{sub 2}, His{sub 2} zinc finger motif may be an excellent starting place for the design of new DNA-binding proteins. Continuing studies in this area are sure to reveal new and intriguing insights to our current understanding of the mechanisms of sequence-specific DNA recognition by proteins.
- Research Organization:
- New York Academy of Sciences, New York, NY (United States)
- OSTI ID:
- 134840
- Report Number(s):
- CONF-9307221-; CNN: Grant P01 GM32681; TRN: 95:007741-0006
- Resource Relation:
- Conference: DNA damage: effects on DNA structure and protein recognition, Burlington, VT (United States), 31 Jul - 4 Aug 1993; Other Information: PBD: 1994; Related Information: Is Part Of DNA damage: Effects on DNA structure and protein recognition; Wallace, S.S.; Van Houten, B.; Kow, Yoke Wah [eds.]; PB: 395 p.
- Country of Publication:
- United States
- Language:
- English
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