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| | <StructureSection load='5z7l' size='340' side='right'caption='[[5z7l]], [[Resolution|resolution]] 2.02Å' scene=''> | | <StructureSection load='5z7l' size='340' side='right'caption='[[5z7l]], [[Resolution|resolution]] 2.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5z7l]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z7L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5Z7L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z7l]] is a 4 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=5Z7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z7L 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]] 2.02Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5z7g|5z7g]], [[5z7a|5z7a]]</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'>[http://proteopedia.org/fgij/fg.htm?mol=5z7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z7l OCA], [http://pdbe.org/5z7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z7l RCSB], [http://www.ebi.ac.uk/pdbsum/5z7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z7l 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=5z7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z7l OCA], [https://pdbe.org/5z7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z7l RCSB], [https://www.ebi.ac.uk/pdbsum/5z7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z7l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CACO2_HUMAN CACO2_HUMAN]] May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion.<ref>PMID:17635994</ref> [[http://www.uniprot.org/uniprot/AZI2_HUMAN AZI2_HUMAN]] Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1.<ref>PMID:14560022</ref> <ref>PMID:15611223</ref> <ref>PMID:21931631</ref> | + | [https://www.uniprot.org/uniprot/CACO2_HUMAN CACO2_HUMAN] May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion.<ref>PMID:17635994</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
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| - | NDP52 and TAX1BP1, two SKIP carboxyl homology (SKICH) domain-containing autophagy receptors, play crucial roles in selective autophagy. The autophagic functions of NDP52 and TAX1BP1 are regulated by TANK-binding kinase 1 (TBK1), which may associate with them through the adaptor NAP1. However, the molecular mechanism governing the interactions of NAP1 with NDP52 and TAX1BP1, as well as the effects induced by TBK1-mediated phosphorylation of NDP52 and TAX1BP1, remains elusive. Here, we report the atomic structures of the SKICH regions of NDP52 and TAX1BP1 in complex with NAP1, which not only uncover the mechanistic bases underpinning the specific interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1 but also reveal the binding mode of a SKICH domain. Moreover, we uncovered that the SKICH domains of NDP52 and TAX1BP1 share a general binding mode to interact with NAP1. Finally, we also evaluated the currently known TBK1-mediated phosphorylation sites in the SKICH domains of NDP52 and TAX1BP1 on the basis of their interactions with NAP1. In all, our findings provide mechanistic insights into the interactions of NAP1 with NDP52 and TAX1BP1, and are valuable for further understanding the functions of these proteins in selective autophagy.
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| - | Mechanistic insights into the interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1.,Fu T, Liu J, Wang Y, Xie X, Hu S, Pan L Proc Natl Acad Sci U S A. 2018 Dec 11;115(50):E11651-E11660. doi:, 10.1073/pnas.1811421115. Epub 2018 Nov 20. PMID:30459273<ref>PMID:30459273</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 5z7l" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fu, T]] | + | [[Category: Fu T]] |
| - | [[Category: Pan, L F]] | + | [[Category: Pan LF]] |
| - | [[Category: Autophagy]]
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| - | [[Category: Nap1]]
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| - | [[Category: Ndp52]]
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| - | [[Category: Signaling protein]]
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| - | [[Category: Skich]]
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