5X3Z

Solution structure of musashi1 RBD2 in complex with RNA


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

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

Iwaoka, R.Nagata, T.Tsuda, K.Imai, T.Okano, H.Kobayashi, N.Katahira, M.

(2017) Molecules 22

  • DOI: https://doi.org/10.3390/molecules22071207
  • Primary Citation of Related Structures:  
    5X3Y, 5X3Z

  • 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}- 15 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 ( n ) of the linker up to n = 50 may be possible.


  • Organizational Affiliation

    Institute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan. iwaoka.ryo.g78@kyoto-u.jp.


Macromolecules

Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
RNA-binding protein Musashi homolog 196Mus musculusMutation(s): 0 
Gene Names: Msi1Msi1h
UniProt
Find proteins for Q61474 (Mus musculus)
Explore Q61474 
Go to UniProtKB:  Q61474
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ61474
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
RNA (5'-R(*GP*UP*AP*GP*U)-3')5Mus musculus
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
JSPSJapan15H01256
JSPSJapan16H00833
JSPSJapan16K14678
JSPSJapan15H01634
JSPSJapan26440026

Revision History  (Full details and data files)

  • Version 1.0: 2017-12-13
    Type: Initial release