View source for 3vtu


==Crystal structure of human LC3B_2-119==
<StructureSection load='3vtu' size='340' side='right'caption='[[3vtu]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vtu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VTU 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3vtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vtu OCA], [https://pdbe.org/3vtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vtu RCSB], [https://www.ebi.ac.uk/pdbsum/3vtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vtu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MLP3B_HUMAN MLP3B_HUMAN] Involved in formation of autophagosomal vacuoles (autophagosomes).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Selective autophagy is mediated by the interaction of autophagy modifiers and autophagy receptors that also bind to ubiquitinated cargo. Optineurin is an autophagy receptor that plays a role in the clearance of cytosolic Salmonella. The interaction between receptors and modifiers is often relatively weak, with typical values for the dissociation constant in the low micromolar range. The interaction of optineurin with autophagy modifiers is even weaker but can be significantly enhanced through phosphorylation by the TANK binding kinase 1. Here we present the NMR and crystal structures of the autophagy modifier LC3B in complex with the LC3 interaction region of optineurin either phosphorylated or bearing phospho-mimicking mutations. The structures show that the negative charge induced by phosphorylation is recognized by the side-chains of Arg11 and Lys51 in LC3B. Further mutational analysis suggests that the replacement of the canonical Trp side chain of autophagy receptors with the smaller Phe side chain in optineurin significantly weakens its interaction with the autophagy modifier LC3B. Through phosphorylation of serines directly N-terminally located to the Phe residue, the affinity is increased to the level normally seen for receptor - modifier interactions. Phosphorylation, therefore, acts as a switch for optineurin-based selective autophagy.

Structural basis for phosphorylation-triggered autophagic clearance of Salmonella.,Rogov VV, Suzuki H, Fiskin E, Wild P, Kniss A, Rozenknop A, Kato R, Kawasaki M, McEwan DG, Lohr F, Guntert P, Dikic I, Wakatsuki S, Dotsch V Biochem J. 2013 Jun 28. PMID:23805866<ref>PMID:23805866</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vtu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kato R]]
[[Category: Kawasaki M]]
[[Category: Suzuki H]]
[[Category: Wakatsuki S]]