Download MendeleyA Cys3His Zinc-Binding Domain from Nup475/Tristetraproline: a Novel Fold with a Disklike Structure
Amann, B.T., Worthington, M.T., Berg, J.M.(2003) Biochemistry 42: 217-221
- PubMed: 12515557
- DOI: https://doi.org/10.1021/bi026988m
- Primary Citation of Related Structures:
1M9O - PubMed Abstract:
Nup475 (also known as tristetraprolin and TIS11) includes two zinc-binding domains of the form Cys-X8-Cys-X5-Cys-X3-His. These domains are required for rapid degradation of tumor necrosis factor (TNF) and other mRNAs through the interaction with AU-rich elements in their 3'-untranslated regions. The three-dimensional solution structure of the first domain was determined by multidimensional nuclear magnetic resonance spectroscopy, revealing a novel fold around a central zinc ion. The core structure is disk-like with a diameter of approximately 25 A and a width of approximately 12 A. This structure provides a basis for evaluating the role of individual residues for structural stability and for nucleic acid binding.
Organizational Affiliation:
Department of Biophysics and Biophysical Chemistry, 713 WBSB, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.
