The papillomavirus E2 proteins: structure, function, and biology.
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.
Hegde
Rashmi S
RS
Division of Developmental Biology, Childrens Hospital Research Foundation, 3333 Burnet Avenue, Cincinnati, OH 45229-3039, USA. rashmi.hegde@chmcc.org
D008958:Models, Molecular; D027383:Papillomaviridae / Q000378:metabolism*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*
D014764:Viral Proteins