Journal
SCIENCE
Volume 305, Issue 5682, Pages 386-389Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1097064
Keywords
-
Categories
Funding
- NIGMS NIH HHS [GM 23467] Funding Source: Medline
Ask authors/readers for more resources
Interaction of regulatory DNA binding proteins with their target sites is usually preceded by binding to nonspecific DNA. This speeds up the search for the target site by several orders of magnitude. We report the solution structure and dynamics of the complex of a dimeric lac repressor DNA binding domain with nonspecific DNA. The same set of residues can switch roles from a purely electrostatic interaction with the DNA backbone in the nonspecific complex to a highly specific binding mode with the base pairs of the cognate operator sequence. The protein DNA interface of the nonspecific complex is flexible on biologically relevant time scales that may assist in the rapid and efficient finding of the target site.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available