5X3Y
Refined solution structure of musashi1 RBD2
Summary for 5X3Y
| Entry DOI | 10.2210/pdb5x3y/pdb |
| Related | 5X3Z |
| NMR Information | BMRB: 36058 |
| Descriptor | RNA-binding protein Musashi homolog 1 (1 entity in total) |
| Functional Keywords | rna-binding protein, rrm, rbd, rna binding protein |
| Biological source | Mus musculus (Mouse) |
| Cellular location | Cytoplasm : Q61474 |
| Total number of polymer chains | 1 |
| Total formula weight | 10945.51 |
| Authors | Iwaoka, R.,Nagata, T.,Tsuda, K.,Imai, T.,Okano, H.,Kobayashi, N.,Katahira, M. (deposition date: 2017-02-09, release date: 2017-12-13, Last modification date: 2024-05-01) |
| Primary citation | Iwaoka, R.,Nagata, T.,Tsuda, K.,Imai, T.,Okano, H.,Kobayashi, N.,Katahira, M. Structural Insight into the Recognition of r(UAG) by Musashi-1 RBD2, and Construction of a Model of Musashi-1 RBD1-2 Bound to the Minimum Target RNA Molecules, 22:-, 2017 Cited by PubMed Abstract: Musashi-1 (Msi1) controls the maintenance of stem cells and tumorigenesis through binding to its target mRNAs and subsequent translational regulation. Msi1 has two RNA-binding domains (RBDs), RBD1 and RBD2, which recognize r(GUAG) and r(UAG), respectively. These minimal recognition sequences are connected by variable linkers in the Msi1 target mRNAs, however, the molecular mechanism by which Msi1 recognizes its targets is not yet understood. We previously determined the solution structure of the Msi1 RBD1:r(GUAGU) complex. Here, we determined the first structure of the RBD2:r(GUAGU) complex. The structure revealed that the central trinucleotide, r(UAG), is specifically recognized by the intermolecular hydrogen-bonding and aromatic stacking interactions. Importantly, the C-terminal region, which is disordered in the free form, took a certain conformation, resembling a helix. The observation of chemical shift perturbation and intermolecular NOEs, together with increases in the heteronuclear steady-state {¹H}-N NOE values on complex formation, indicated the involvement of the C-terminal region in RNA binding. On the basis of the two complex structures, we built a structural model of consecutive RBDs with r(UAGGUAG) containing both minimal recognition sequences, which resulted in no steric hindrance. The model suggests recognition of variable lengths () of the linker up to = 50 may be possible. PubMed: 28753936DOI: 10.3390/molecules22071207 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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