1m9o | pdb_00001m9o
NMR structure of the first Zinc Binding domain of Nup475/TTP/TIS11
Structural highlights
FunctionTTP_MOUSE mRNA-binding protein involved in post-transcriptional regulation of AU-rich element (ARE)-containing mRNAs. Acts by specifically binding ARE-containing mRNAs and promoting their degradation. Plays a key role in the post-transcriptional regulation of tumor necrosis factor (TNF).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNup475 (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. A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure.,Amann BT, Worthington MT, Berg JM Biochemistry. 2003 Jan 14;42(1):217-21. PMID:12515557[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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