5e6n: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of C. elegans LGG-2==
<StructureSection load='5e6n' size='340' side='right' caption='[[5e6n]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5e6n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6N FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e6o|5e6o]]</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=5e6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6n OCA], [http://pdbe.org/5e6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6n RCSB], [http://www.ebi.ac.uk/pdbsum/5e6n PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/LGG2_CAEEL LGG2_CAEEL]] Ubiquitin-like modifier involved in autophagy and essential for dauer development and life-span extension.<ref>PMID:20523114</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multicellular organisms have multiple homologs of the yeast ATG8 gene, but the differential roles of these homologs in autophagy during development remain largely unknown. Here we investigated structure/function relationships in the two C. elegans Atg8 homologs, LGG-1 and LGG-2. lgg-1 is essential for degradation of protein aggregates, while lgg-2 has cargo-specific and developmental-stage-specific roles in aggregate degradation. Crystallography revealed that the N-terminal tails of LGG-1 and LGG-2 adopt the closed and open form, respectively. LGG-1 and LGG-2 interact differentially with autophagy substrates and Atg proteins, many of which carry a LIR motif. LGG-1 and LGG-2 have structurally distinct substrate binding pockets that prefer different residues in the interacting LIR motif, thus influencing binding specificity. Lipidated LGG-1 and LGG-2 possess distinct membrane tethering and fusion activities, which may result from the N-terminal differences. Our study reveals the differential function of two ATG8 homologs in autophagy during C. elegans development.


The entry 5e6n is ON HOLD  until Paper Publication
Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.,Wu F, Watanabe Y, Guo XY, Qi X, Wang P, Zhao HY, Wang Z, Fujioka Y, Zhang H, Ren JQ, Fang TC, Shen YX, Feng W, Hu JJ, Noda NN, Zhang H Mol Cell. 2015 Dec 17;60(6):914-29. doi: 10.1016/j.molcel.2015.11.019. PMID:26687600<ref>PMID:26687600</ref>


Authors: Qi, X., Ren, J.Q., Wu, F., Zhang, H., Feng, W.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of C. elegans LGG-2
<div class="pdbe-citations 5e6n" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
[[Category: Ren, J.Q]]
<references/>
[[Category: Zhang, H]]
__TOC__
</StructureSection>
[[Category: Feng, W]]
[[Category: Qi, X]]
[[Category: Qi, X]]
[[Category: Feng, W]]
[[Category: Ren, J Q]]
[[Category: Wu, F]]
[[Category: Wu, F]]
[[Category: Zhang, H]]
[[Category: Atg8 protein family]]
[[Category: Protein binding]]
[[Category: Ubiquitin-like protein]]
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