View source for 2ncn


==Solution Structure of the Autophagy-Related Protein LC3C==
<StructureSection load='2ncn' size='340' side='right'caption='[[2ncn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ncn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NCN FirstGlance]. <br>
</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=2ncn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ncn OCA], [https://pdbe.org/2ncn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ncn RCSB], [https://www.ebi.ac.uk/pdbsum/2ncn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ncn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MLP3C_HUMAN MLP3C_HUMAN] Ubiquitin-like modifier that plays a crucial role in antibacterial autophagy (xenophagy) through the selective binding of CALCOCO2. Recruites all ATG8 family members to infecting bacteria such as S.Typhimurium.<ref>PMID:23022382</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
(Macro-)autophagy is a compartmental degradation pathway conserved from yeast to mammals. The yeast protein Atg8 mediates membrane tethering/hemifusion and cargo recruitment and is essential for autophagy. The human MAP1LC3/GABARAP family proteins show high sequence identity with Atg8, but MAP1LC3C is distinguished by a conspicuous amino-terminal extension with unknown functional significance. We have determined the high-resolution three-dimensional structure and measured the backbone dynamics of MAP1LC3C by NMR spectroscopy. From Ser18 to Ala120, MAP1LC3C forms an alpha-helix followed by the ubiquitin-like tertiary fold with two hydrophobic binding pockets used by MAP1LC3/GABARAP proteins to recognize targets presenting LC3-interacting regions (LIRs). Unlike other MAP1LC3/GABARAP proteins, the amino-terminal region of MAP1LC3C does not form a stable helix alpha1 but a "sticky arm" consisting of a polyproline II motif on a flexible linker. Ser18 at the interface between this linker and the structural core can be phosphorylated in vitro by protein kinase A, which causes additional conformational heterogeneity as monitored by NMR spectroscopy and molecular dynamics simulations, including changes in the LIR-binding interface. Based on these results we propose that the amino-terminal polyproline II motif mediates specific interactions with the microtubule cytoskeleton and that Ser18 phosphorylation modulates the interplay of MAP1LC3C with its various target proteins.

Solution structure of the autophagy-related protein LC3C reveals a polyproline II motif on a mobile tether with phosphorylation site.,Krichel C, Mockel C, Schillinger O, Huesgen PF, Sticht H, Strodel B, Weiergraber OH, Willbold D, Neudecker P Sci Rep. 2019 Oct 2;9(1):14167. doi: 10.1038/s41598-019-48155-8. PMID:31578424<ref>PMID:31578424</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2ncn" style="background-color:#fffaf0;"></div>

==See Also==
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Krichel C]]
[[Category: Neudecker P]]
[[Category: Weiergraeber OH]]
[[Category: Willbold D]]