Solution structure of the c-terminal core domain of human TFIIB: Similarity to cyclin A and interaction with TATA-binding protein

117Citations
Citations of this article
33Readers
Mendeley users who have this article in their library.
Get full text

Abstract

TFIIB is an essential component of the machinery that transcribes protein-coding genes. The three-dimensional structure of the human TFIIB core domain (TFIIBc) has been determined using multidimensional heteronuclear magnetic resonance spectroscopy. The molecule consists of two direct repeats that adopt similar α-helical folds, conferring pseudo-twofold symmetry. An extensive, central basic surface including an amphipathic a helix is critical to the function of TFIIB as a bridge between the TBP-promoter complex and RNA polymerase II and associated general and regulatory transcription factors. Similarities between the TFIIBc and cyclin A folds indicate that elements of the eukaryotic cell cycle control apparatus evolved from more fundamental transcriptional control components, demonstrating a link between the transcription and cell cycle molecular machineries. © 1995.

Cite

CITATION STYLE

APA

Bagby, S., Kim, S., Maldonado, E., Tong, K. I., Reinberg, D., & Ikura, M. (1995). Solution structure of the c-terminal core domain of human TFIIB: Similarity to cyclin A and interaction with TATA-binding protein. Cell, 82(5), 857–867. https://doi.org/10.1016/0092-8674(95)90483-2

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free