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Updated: Sep 27, 2026

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A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure
Barbara T Amann1, Mark T Worthington, Jeremy M Berg
1Department of Biophysics and Biophysical Chemistry, 713 WBSB, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.
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.
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