The Cocrystal Structures of Two Zinc-stabilized DNA-binding Domains Illustrate Different Ways of Achieving Sequence-specific DNA Recognition
This extract was created in the absence of an abstract.
Excerpt
The precise temporal and spatial genetic regulation that underlies the processes of development and differentiation depends on the ability of protein transcription factors to recognize specific DNA-binding sites within the genome. In recognizing a specific DNA sequence, these proteins face a common problem in that they must reach into the major groove of the DNA and interact with a sufficient number of base pairs to uniquely specify the binding site. In addition, they recognize the sequence-dependent structure or defor-mability of the DNA.
Structural studies using both nuclear magnetic resonance (NMR) spectroscopic and X-ray diffraction techniques have revealed that many of these transcription factors achieve sequence-specific recognition through conceptually similar mechanisms: A “reading head” (often α-helical) is positioned in the major groove such that surface amino acids can contact the specific base pairs. Multiple contacts to the phosphate backbone of the DNA not only enhance the binding affinity, but also contribute...
