5cx3
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cx3]] is a 8 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=5CX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CX3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5cx3]] is a 8 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=5CX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CX3 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5cx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cx3 OCA], [https://pdbe.org/5cx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cx3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cx3 ProSAT]</span></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=5cx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cx3 OCA], [https://pdbe.org/5cx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cx3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cx3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MLP3A_HUMAN MLP3A_HUMAN] Involved in formation of autophagosomal vacuoles (autophagosomes). | [https://www.uniprot.org/uniprot/MLP3A_HUMAN MLP3A_HUMAN] Involved in formation of autophagosomal vacuoles (autophagosomes). | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | FYCO1 (FYVE and coiled-coil domain containing 1) functions as an autophagy adaptor in directly linking autophagosomes with the microtubule-based kinesin motor, and plays an essential role in the microtubule plus end-directed transport of autophagic vesicles. The specific association of FYCO1 with autophagosomes is mediated by its interaction with Atg8-family proteins decorated on the outer surface of autophagosome. However, the mechanistic basis governing the interaction between FYCO1 and Atg8-family proteins is largely unknown. Here, using biochemical and structural analyses, we demonstrated that FYCO1 contains a unique LC3-interacting region (LIR), which discriminately binds to mammalian Atg8 orthologs and preferentially binds to the MAP1LC3A and MAP1LC3B. In addition to uncovering the detailed molecular mechanism underlying the FYCO1 LIR and MAP1LC3A interaction, the determined FYCO1-LIR-MAP1LC3A complex structure also reveals a unique LIR binding mode for Atg8-family proteins, and demonstrates, first, the functional relevance of adjacent sequences C-terminal to the LIR core motif for binding to Atg8-family proteins. Taken together, our findings not only provide new mechanistic insight into FYCO1-mediated transport of autophagosomes, but also expand our understanding of the interaction modes between LIR motifs and Atg8-family proteins in general. | ||
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| - | Structural basis of FYCO1 and MAP1LC3A interaction reveals a novel binding mode for Atg8-family proteins.,Cheng X, Wang Y, Gong Y, Li F, Guo Y, Hu S, Liu J, Pan L Autophagy. 2016 Aug 2;12(8):1330-9. doi: 10.1080/15548627.2016.1185590. Epub 2016, May 31. PMID:27246247<ref>PMID:27246247</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5cx3" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]] | *[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of FYCO1 LIR in complex with LC3A
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