2ymj: Difference between revisions
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==Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking.== | |||
<StructureSection load='2ymj' size='340' side='right' caption='[[2ymj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ymj]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YMJ FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bl5|2bl5]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ymj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ymj RCSB], [http://www.ebi.ac.uk/pdbsum/2ymj PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23520467</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Ali, M | [[Category: Ali, M]] | ||
[[Category: Broadhurst, R W | [[Category: Broadhurst, R W]] | ||
[[Category: Hairpin]] | [[Category: Hairpin]] | ||
[[Category: Qki]] | [[Category: Qki]] | ||
[[Category: Star protein]] | [[Category: Star protein]] | ||
[[Category: Translation]] | [[Category: Translation]] |