1M9O
NMR structure of the first Zinc Binding domain of Nup475/TTP/TIS11
Summary for 1M9O
| Entry DOI | 10.2210/pdb1m9o/pdb |
| NMR Information | BMRB: 5525 |
| Descriptor | Tristetraproline, ZINC ION (2 entities in total) |
| Functional Keywords | cys3his type zinc finger, metal binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: P22893 |
| Total number of polymer chains | 1 |
| Total formula weight | 9037.60 |
| Authors | Amann, B.T.,Worthington, M.T.,Berg, J.M. (deposition date: 2002-07-29, release date: 2003-06-03, Last modification date: 2024-05-22) |
| Primary citation | Amann, B.T.,Worthington, M.T.,Berg, J.M. A Cys3His Zinc-Binding Domain from Nup475/Tristetraproline: a Novel Fold with a Disklike Structure Biochemistry, 42:217-221, 2003 Cited by 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. PubMed: 12515557DOI: 10.1021/bi026988m PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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