4oyu: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
New page: '''Unreleased structure''' The entry 4oyu is ON HOLD Authors: Delto, C., Kuper, J., Schindelin, H. Description: Crystal structure of the N-terminal domains of muskelin
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4oyu is ON HOLD
==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 with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4OYU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4oyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oyu OCA], [https://pdbe.org/4oyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oyu RCSB], [https://www.ebi.ac.uk/pdbsum/4oyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oyu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MKLN1_RAT MKLN1_RAT]
<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.


Authors: Delto, C., Kuper, J., Schindelin, H.
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>


Description: Crystal structure of the N-terminal domains of muskelin
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4oyu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Delto C]]
[[Category: Kuper J]]
[[Category: Schindelin H]]
Retrieved from "https://proteopedia.org/4oyu"