MINOR GROOVE-BINDING ARCHITECTURAL PROTEINS - STRUCTURE, FUNCTION, AND DNA RECOGNITION

Citation
Ca. Bewley et al., MINOR GROOVE-BINDING ARCHITECTURAL PROTEINS - STRUCTURE, FUNCTION, AND DNA RECOGNITION, Annual review of biophysics and biomolecular structure, 27, 1998, pp. 105-131
Citations number
63
Categorie Soggetti
Biophysics,Biology
ISSN journal
10568700
Volume
27
Year of publication
1998
Pages
105 - 131
Database
ISI
SICI code
1056-8700(1998)27:<105:MGAP-S>2.0.ZU;2-V
Abstract
To date, high-resolution structures have been solved for five differen t architectural proteins complexed to their DNA target sites. These in clude TATA-box-binding protein, integration host factor (IHF), high mo bility group I(Y)[HMG I(Y)], and the HMG-box-containing proteins SRY a nd LEF-1. Each of these proteins interacts with DNA exclusively throug h minor groove contacts and alters DNA conformation. This paper review s the structural features of these complexes and the roles they play i n facilitating assembly of higher-order protein-DNA complexes and disc usses elements that contribute to sequence-specific recognition and co nformational changes.