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| <StructureSection load='5c50' size='340' side='right'caption='[[5c50]], [[Resolution|resolution]] 1.63Å' scene=''> | | <StructureSection load='5c50' size='340' side='right'caption='[[5c50]], [[Resolution|resolution]] 1.63Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5c50]] is a 2 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=5C50 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C50 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5c50]] is a 2 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=5C50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C50 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</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]] 1.63Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATG101, C12orf44, PP894 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ATG13, KIAA0652 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene></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=5c50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c50 OCA], [http://pdbe.org/5c50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c50 RCSB], [http://www.ebi.ac.uk/pdbsum/5c50 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c50 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=5c50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c50 OCA], [https://pdbe.org/5c50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c50 RCSB], [https://www.ebi.ac.uk/pdbsum/5c50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c50 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ATGA1_HUMAN ATGA1_HUMAN]] Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation.<ref>PMID:19287211</ref> <ref>PMID:19597335</ref> [[http://www.uniprot.org/uniprot/ATG13_HUMAN ATG13_HUMAN]] Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation.<ref>PMID:19287211</ref> <ref>PMID:19211835</ref> <ref>PMID:19225151</ref> <ref>PMID:21855797</ref> <ref>PMID:18936157</ref> <ref>PMID:21795849</ref> | | [https://www.uniprot.org/uniprot/ATGA1_HUMAN ATGA1_HUMAN] Autophagy factor required for autophagosome formation. Stabilizes ATG13, protecting it from proteasomal degradation.<ref>PMID:19287211</ref> <ref>PMID:19597335</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The ULK1 complex, consisting of the ULK1 protein kinase itself, FIP200, Atg13, and Atg101, controls the initiation of autophagy in animals. We determined the structure of the complex of the human Atg13 HORMA (Hop1, Rev7, Mad2) domain in complex with the full-length HORMA domain-only protein Atg101. The two HORMA domains assemble with an architecture conserved in the Mad2 conformational heterodimer and the S. pombe Atg13-Atg101 HORMA complex. The WF finger motif that is essential for function in human Atg101 is sequestered in a hydrophobic pocket, suggesting that the exposure of this motif is regulated. Benzamidine molecules from the crystallization solution mark two hydrophobic pockets that are conserved in, and unique to, animals, and are suggestive of sites that could interact with other proteins. These features suggest that the activity of the animal Atg13-Atg101 subcomplex is regulated and that it is an interaction hub for multiple partners.
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| Structure of the Human Atg13-Atg101 HORMA Heterodimer: an Interaction Hub within the ULK1 Complex.,Qi S, Kim do J, Stjepanovic G, Hurley JH Structure. 2015 Oct 6;23(10):1848-57. doi: 10.1016/j.str.2015.07.011. Epub 2015, Aug 20. PMID:26299944<ref>PMID:26299944</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5c50" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Hurley, J H]] | | [[Category: Hurley JH]] |
| [[Category: Qi, S]] | | [[Category: Qi S]] |
| [[Category: Autophagy]]
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| [[Category: Complex]]
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| [[Category: Horma domain]]
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| [[Category: Protein binding]]
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