4jhr: Difference between revisions

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New page: '''Unreleased structure''' The entry 4jhr is ON HOLD Authors: Zhu Pan, Jinwei Zhu, Yuan Shang, Zhiyi Wei, Min Jia, Caihao Xia, Wenyu Wen, Wenning Wang, Mingjie Zhang Description: An au...
 
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'''Unreleased structure'''


The entry 4jhr is ON HOLD
==An auto-inhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs==
<StructureSection load='4jhr' size='340' side='right'caption='[[4jhr]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jhr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JHR 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]] 2.8&#8491;</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=4jhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jhr OCA], [https://pdbe.org/4jhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jhr RCSB], [https://www.ebi.ac.uk/pdbsum/4jhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jhr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GPSM2_MOUSE GPSM2_MOUSE] Plays an important role in spindle pole orientation (By similarity). Interacts and contributes to the functional activity of G(i) alpha proteins. Acts to stabilize the apical complex during neuroblast divisions.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
LGN plays essential roles in asymmetric cell divisions via its N-terminal TPR-motif-mediated binding to mInsc and NuMA. This scaffolding activity requires the release of the autoinhibited conformation of LGN by binding of Galphai to its C-terminal GoLoco (GL) motifs. The interaction between the GL and TPR motifs of LGN represents a distinct GL/target binding mode with an unknown mechanism. Here, we show that two consecutive GL motifs of LGN form a minimal TPR-motif-binding unit. GL12 and GL34 bind to TPR0-3 and TPR4-7, respectively. The crystal structure of a truncated LGN reveals that GL34 forms a pair of parallel alpha helices and binds to the concave surface of TPR4-7, thereby preventing LGN from binding to other targets. Importantly, the GLs bind to TPR motifs with a mode distinct from that observed in the GL/Galphai.GDP complexes. Our results also indicate that multiple and orphan GL motif proteins likely respond to G proteins with distinct mechanisms.


Authors: Zhu Pan, Jinwei Zhu, Yuan Shang, Zhiyi Wei, Min Jia, Caihao Xia, Wenyu Wen, Wenning Wang, Mingjie Zhang
An Autoinhibited Conformation of LGN Reveals a Distinct Interaction Mode between GoLoco Motifs and TPR Motifs.,Pan Z, Zhu J, Shang Y, Wei Z, Jia M, Xia C, Wen W, Wang W, Zhang M Structure. 2013 Jun 4;21(6):1007-17. doi: 10.1016/j.str.2013.04.005. Epub 2013, May 9. PMID:23665171<ref>PMID:23665171</ref>


Description: An auto-inhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4jhr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Jia M]]
[[Category: Pan Z]]
[[Category: Shang Y]]
[[Category: Wang W]]
[[Category: Wei Z]]
[[Category: Wen W]]
[[Category: Xia C]]
[[Category: Zhang M]]
[[Category: Zhu J]]

Latest revision as of 14:23, 8 November 2023

An auto-inhibited conformation of LGN reveals a distinct interaction mode between GoLoco motifs and TPR motifs

4jhr, resolution 2.80Å

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