2RV5
Solution structures of the DNA-binding domain (ZF8) of mouse immune-related zinc-finger protein ZFAT
Summary for 2RV5
| Entry DOI | 10.2210/pdb2rv5/pdb |
| Related | 2RUT 2RUU 2RUV 2RUW 2RUX 2RUY 2RUZ 2RV0 2RV1 2RV2 2RV3 2RV4 2RV6 2RV7 2elx |
| NMR Information | BMRB: 11485 |
| Descriptor | Zinc finger protein ZFAT, ZINC ION (2 entities in total) |
| Functional Keywords | zfat, zinc finger, transcription |
| Biological source | Mus musculus (mouse) |
| Cellular location | Nucleus : Q7TS63 |
| Total number of polymer chains | 1 |
| Total formula weight | 3777.70 |
| Authors | Tochio, N.,Umehara, T.,Kigawa, T.,Yokoyama, S. (deposition date: 2015-01-26, release date: 2015-04-08, Last modification date: 2024-05-01) |
| Primary citation | Tochio, N.,Umehara, T.,Nakabayashi, K.,Yoneyama, M.,Tsuda, K.,Shirouzu, M.,Koshiba, S.,Watanabe, S.,Kigawa, T.,Sasazuki, T.,Shirasawa, S.,Yokoyama, S. Solution structures of the DNA-binding domains of immune-related zinc-finger protein ZFAT J.Struct.Funct.Genom., 16:55-65, 2015 Cited by PubMed Abstract: ZFAT is a transcriptional regulator, containing eighteen C2H2-type zinc-fingers and one AT-hook, involved in autoimmune thyroid disease, apoptosis, and immune-related cell survival. We determined the solution structures of the thirteen individual ZFAT zinc-fingers (ZF) and the tandemly arrayed zinc-fingers in the regions from ZF2 to ZF5, by NMR spectroscopy. ZFAT has eight uncommon bulged-out helix-containing zinc-fingers, and six of their structures (ZF4, ZF5, ZF6, ZF10, ZF11, and ZF13) were determined. The distribution patterns of the putative DNA-binding surface residues are different among the ZFAT zinc-fingers, suggesting the distinct DNA sequence preferences of the N-terminal and C-terminal zinc-fingers. Since ZFAT has three to five consecutive tandem zinc-fingers, which may cooperatively function as a unit, we also determined two tandemly arrayed zinc-finger structures, between ZF2 to ZF4 and ZF3 to ZF5. Our NMR spectroscopic analysis detected the interaction between ZF4 and ZF5, which are connected by an uncommon linker sequence, KKIK. The ZF4-ZF5 linker restrained the relative structural space between the two zinc-fingers in solution, unlike the other linker regions with determined structures, suggesting the involvement of the ZF4-ZF5 interfinger linker in the regulation of ZFAT function. PubMed: 25801860DOI: 10.1007/s10969-015-9196-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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