2ymj

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.

Structural highlights

2ymj is a 2 chain structure with sequence from Xenopus laevis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

QKIA_XENLA RNA-binding protein that plays a central role in myelinization. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Acts by regulating pre-mRNA splicing, mRNA export, mRNA stability and protein translation. Required to protect and promote stability of mRNAs which promotes oligodendrocyte differentiation. Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of some pre-mRNA. Acts as a translational repressor (By similarity). Essential for notochord development.^[1]

Publication Abstract from PubMed

The STAR protein family member Quaking is essential for early development in vertebrates. For example, in oligodendrocyte cells it regulates the splicing, localization, translation and lifetime of a set of mRNAs that code for crucial components of myelin. The Quaking protein contains three contiguous conserved regions: a QUA1 oligomerization element, followed by a single-stranded RNA binding motif comprising the KH and QUA2 domains. An embryonic lethal point mutation in the QUA1 domain, E48G, is known to affect both the aggregation state and RNA-binding properties of the murine Quaking ortholog (QKI). Here we report the NMR solution structure of the QUA1 domain from the Xenopus laevis Quaking ortholog (pXqua), which forms a dimer composed of two perpendicularly docked alpha-helical hairpin motifs. Size exclusion chromatography studies of a range of mutants demonstrate that the dimeric state of the pXqua QUA1 domain is stabilized by a network of interactions between side-chains, with significant roles played by an intra-molecular hydrogen bond between Y41 and E72 (the counterpart to QKI E48) and an inter-protomer salt bridge between E72 and R67. These results are compared with recent structural and mutagenesis studies of QUA1 domains from the STAR family members QKI, GLD-1 and Sam68.

Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.,Ali M, Broadhurst RW PLoS One. 2013;8(3):e57345. doi: 10.1371/journal.pone.0057345. Epub 2013 Mar 8. PMID:23520467^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zorn AM, Krieg PA. The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos. Genes Dev. 1997 Sep 1;11(17):2176-90. PMID:9303534
↑ Ali M, Broadhurst RW. Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking. PLoS One. 2013;8(3):e57345. doi: 10.1371/journal.pone.0057345. Epub 2013 Mar 8. PMID:23520467 doi:http://dx.doi.org/10.1371/journal.pone.0057345

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ymj"

Categories: Large Structures | Xenopus laevis | Ali M | Broadhurst RW

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2ymj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YMJ FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ymj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymj OCA], [https://pdbe.org/2ymj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ymj RCSB], [https://www.ebi.ac.uk/pdbsum/2ymj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ymj ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ymj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymj OCA], [https://pdbe.org/2ymj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ymj RCSB], [https://www.ebi.ac.uk/pdbsum/2ymj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ymj ProSAT]</span></td></tr>
 </table>
 == Function ==

2ymj

From Proteopedia

Current revision

Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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