Electronic Resource
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Biophysics and Biomolecular Structure
31 (2002), S. 343-360
ISSN:
1056-8700
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Biology
,
Physics
Notes:
Abstract Nearly twenty years after the first high-resolution crystal structures of specific protein-DNA complexes were determined, the stereo-chemical basis for protein-DNA recognition remains an active area of investigation. One outstanding question is, how are proteins able to detect noncontacted sequences in their binding sites? The papillomavirus E2 proteins represent a particularly suitable group of proteins in which to examine the mechanisms of "indirect readout." Coordinated structural and thermodynamic studies of the E2-DNA interaction conducted over the past five years are summarized in this review. The data support a model in which the electrostatic properties of the individual E2 proteins correlate with their affinities for intrinsically flexible or rigidly prebent DNA targets.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.biophys.31.100901.142129
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