7FBV
The solution structure of the second RRM domain of Matrin-3
Summary for 7FBV
| Entry DOI | 10.2210/pdb7fbv/pdb |
| NMR Information | BMRB: 36431 |
| Descriptor | Matrin-3 (1 entity in total) |
| Functional Keywords | rrm, als/ftd, nuclear matrix protein, structural genomics, psi-2, protein structure initiative, riken structural genomics/proteomics initiative, rsgi, rna binding protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 12499.46 |
| Authors | Muto, Y.,Kobayashi, N.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2021-07-13, release date: 2022-02-16, Last modification date: 2024-05-15) |
| Primary citation | He, F.,Kuwasako, K.,Takizawa, M.,Takahashi, M.,Tsuda, K.,Nagata, T.,Watanabe, S.,Tanaka, A.,Kobayashi, N.,Kigawa, T.,Guntert, P.,Shirouzu, M.,Yokoyama, S.,Muto, Y. 1 H, 13 C and 15 N resonance assignments and solution structures of the two RRM domains of Matrin-3. Biomol.Nmr Assign., 16:41-49, 2022 Cited by PubMed Abstract: Matrin-3 is a multifunctional protein that binds to both DNA and RNA. Its DNA-binding activity is linked to the formation of the nuclear matrix and transcriptional regulation, while its RNA-binding activity is linked to mRNA metabolism including splicing, transport, stabilization, and degradation. Correspondingly, Matrin-3 has two zinc finger domains for DNA binding and two consecutive RNA recognition motif (RRM) domains for RNA binding. Matrin-3 has been reported to cause amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) when its disordered region contains pathogenic mutations. Simultaneously, it has been shown that the RNA-binding activity of Matrin-3 mediated by its RRM domains, affects the formation of insoluble cytoplasmic granules, which are related to the pathogenic mechanism of ALS/FTD. Thus, the effect of the RRM domains on the phase separation of condensed protein/RNA mixtures has to be clarified for a comprehensive understanding of ALS/FTD. Here, we report the H, N, and C resonance assignments of the two RNA binding domains and their solution structures. The resonance assignments and the solution structures obtained in this work will contribute to the elucidation of the molecular basis of Matrin-3 in the pathogenic mechanism of ALS and/or FTD. PubMed: 34783967DOI: 10.1007/s12104-021-10057-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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