4oyu: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of the N-terminal domains of muskelin==
<StructureSection load='4oyu' size='340' side='right' caption='[[4oyu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4oyu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OYU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4oyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oyu RCSB], [http://www.ebi.ac.uk/pdbsum/4oyu PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Neurons regulate the number of surface receptors by balancing the transport to and from the plasma membrane to adjust their signaling properties. The protein muskelin was recently identified as a key factor guiding the transport of alpha1 subunit-containing GABAA receptors. Here we present the crystal structure of muskelin, comprising its N-terminal discoidin domain and Lis1-homology (LisH) motif. The molecule crystallized as a dimer with the LisH motif exclusively mediating oligomerization. Our subsequent biochemical analyses confirmed that the LisH motif acts as a dimerization element in muskelin. Together with an intermolecular head-to-tail interaction, the LisH-dependent dimerization is required to assemble a muskelin tetramer. Intriguingly, our cellular studies revealed that the loss of this dimerization results in a complete redistribution of muskelin from the cytoplasm to the nucleus and impairs muskelin's function in GABAA receptor transport. These studies demonstrate that the LisH-dependent dimerization is a crucial factor for muskelin function.


The entry 4oyu is ON HOLD  until Paper Publication
The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization.,Delto CF, Heisler FF, Kuper J, Sander B, Kneussel M, Schindelin H Structure. 2015 Feb 3;23(2):364-73. doi: 10.1016/j.str.2014.11.016. Epub 2015 Jan, 8. PMID:25579817<ref>PMID:25579817</ref>


Authors: Delto, C., Kuper, J., Schindelin, H.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of the N-terminal domains of muskelin
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Delto, C]]
[[Category: Delto, C]]
[[Category: Kuper, J]]
[[Category: Schindelin, H]]
[[Category: Schindelin, H]]
[[Category: Kuper, J]]
[[Category: Dimer]]
[[Category: Discoidin domain]]
[[Category: Lish motif]]
[[Category: Protein binding]]
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