MINOR GROOVE-BINDING ARCHITECTURAL PROTEINS: Structure, Function, and DNA Recognition
- 1 June 1998
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biophysics
- Vol. 27 (1), 105-131
- https://doi.org/10.1146/annurev.biophys.27.1.105
Abstract
▪ Abstract To date, high-resolution structures have been solved for five different architectural proteins complexed to their DNA target sites. These include TATA-box–binding protein, integration host factor (IHF), high mobility group I(Y)[HMG I(Y)], and the HMG-box–containing proteins SRY and LEF-1. Each of these proteins interacts with DNA exclusively through minor groove contacts and alters DNA conformation. This paper reviews the structural features of these complexes and the roles they play in facilitating assembly of higher-order protein–DNA complexes and discusses elements that contribute to sequence-specific recognition and conformational changes.Keywords
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