4oyu

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'''Unreleased structure'''
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==Crystal structure of the N-terminal domains of muskelin==
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<StructureSection load='4oyu' size='340' side='right' caption='[[4oyu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4oyu is ON HOLD until Paper Publication
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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>
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Authors: Delto, C., Kuper, J., Schindelin, H.
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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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Description: Crystal structure of the N-terminal domains of muskelin
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Delto, C]]
[[Category: Delto, C]]
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[[Category: Kuper, J]]
[[Category: Schindelin, H]]
[[Category: Schindelin, H]]
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[[Category: Kuper, J]]
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[[Category: Dimer]]
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[[Category: Discoidin domain]]
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[[Category: Lish motif]]
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[[Category: Protein binding]]

Revision as of 11:45, 12 February 2015

Crystal structure of the N-terminal domains of muskelin

4oyu, resolution 1.80Å

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