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| | <StructureSection load='5cx3' size='340' side='right'caption='[[5cx3]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5cx3' size='340' side='right'caption='[[5cx3]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cx3]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/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"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAP1LC3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FYCO1, ZFYVE7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cx3 OCA], [http://pdbe.org/5cx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cx3 RCSB], [http://www.ebi.ac.uk/pdbsum/5cx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cx3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/FYCO1_HUMAN FYCO1_HUMAN]] Nuclear cataract. The disease is caused by mutations affecting the gene represented in this entry. Pathogenic mutations in FYCO1 can affect intracellular transport of autophagocytic vesicles from the perinuclear area to the periphery, leading to an accumulation of large numbers of vesicles and hence loss of lens transparency (PubMed:21636066).<ref>PMID:21636066</ref> | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MLP3A_HUMAN MLP3A_HUMAN]] Involved in formation of autophagosomal vacuoles (autophagosomes). [[http://www.uniprot.org/uniprot/FYCO1_HUMAN FYCO1_HUMAN]] May mediate microtubule plus end-directed vesicle transport.<ref>PMID:20100911</ref> | + | [https://www.uniprot.org/uniprot/MLP3A_HUMAN MLP3A_HUMAN] Involved in formation of autophagosomal vacuoles (autophagosomes). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cheng, X]] | + | [[Category: Cheng X]] |
| - | [[Category: Pan, L]] | + | [[Category: Pan L]] |
| - | [[Category: Autophagy adaptor]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
MLP3A_HUMAN Involved in formation of autophagosomal vacuoles (autophagosomes).
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cheng X, Wang Y, Gong Y, Li F, Guo Y, Hu S, Liu J, Pan L. Structural basis of FYCO1 and MAP1LC3A interaction reveals a novel binding mode for Atg8-family proteins. Autophagy. 2016 Aug 2;12(8):1330-9. doi: 10.1080/15548627.2016.1185590. Epub 2016, May 31. PMID:27246247 doi:http://dx.doi.org/10.1080/15548627.2016.1185590
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