5x3y

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Current revision (07:28, 1 May 2024) (edit) (undo)
 
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==Refined solution structure of musashi1 RBD2==
==Refined solution structure of musashi1 RBD2==
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<StructureSection load='5x3y' size='340' side='right'caption='[[5x3y]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5x3y' size='340' side='right'caption='[[5x3y]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5x3y]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X3Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X3Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5x3y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X3Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X3Y FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x3z|5x3z]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x3y OCA], [http://pdbe.org/5x3y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x3y RCSB], [http://www.ebi.ac.uk/pdbsum/5x3y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x3y ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5x3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x3y OCA], [https://pdbe.org/5x3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x3y RCSB], [https://www.ebi.ac.uk/pdbsum/5x3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x3y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MSI1H_MOUSE MSI1H_MOUSE]] RNA binding protein that regulates the expression of target mRNAs at the translation level. Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May play a role in the proliferation and maintenance of stem cells in the central nervous system.<ref>PMID:11359897</ref> <ref>PMID:12407178</ref>
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[https://www.uniprot.org/uniprot/MSI1H_MOUSE MSI1H_MOUSE] RNA binding protein that regulates the expression of target mRNAs at the translation level. Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May play a role in the proliferation and maintenance of stem cells in the central nervous system.<ref>PMID:11359897</ref> <ref>PMID:12407178</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 {(1)H}-(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.
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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 Molecules. 2017 Jul 19;22(7). pii: molecules22071207. doi:, 10.3390/molecules22071207. PMID:28753936<ref>PMID:28753936</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5x3y" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Imai, T]]
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[[Category: Mus musculus]]
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[[Category: Iwaoka, R]]
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[[Category: Imai T]]
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[[Category: Katahira, M]]
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[[Category: Iwaoka R]]
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[[Category: Kobayashi, N]]
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[[Category: Katahira M]]
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[[Category: Nagata, T]]
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[[Category: Kobayashi N]]
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[[Category: Okano, H]]
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[[Category: Nagata T]]
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[[Category: Tsuda, K]]
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[[Category: Okano H]]
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[[Category: Rbd]]
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[[Category: Tsuda K]]
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[[Category: Rna binding protein]]
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[[Category: Rna-binding protein]]
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[[Category: Rrm]]
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Current revision

Refined solution structure of musashi1 RBD2

PDB ID 5x3y

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