7eaa
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==crystal structure of NDP52 SKICH domain in complex with RB1CC1 coiled-coil domain== |
| - | <StructureSection load='7eaa' size='340' side='right'caption='[[7eaa]]' scene=''> | + | <StructureSection load='7eaa' size='340' side='right'caption='[[7eaa]], [[Resolution|resolution]] 2.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7eaa]] 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=7EAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EAA 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=7eaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eaa OCA], [https://pdbe.org/7eaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eaa RCSB], [https://www.ebi.ac.uk/pdbsum/7eaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eaa ProSAT]</span></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]] 2.6Å</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=7eaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eaa OCA], [https://pdbe.org/7eaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eaa RCSB], [https://www.ebi.ac.uk/pdbsum/7eaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eaa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RBCC1_HUMAN RBCC1_HUMAN] Involved in autophagy (PubMed:21775823). Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1 (PubMed:23392225). Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy (By similarity). Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis (By similarity). Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways (PubMed:10769033, PubMed:12221124). Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111 (By similarity). Functions as a DNA-binding transcription factor (PubMed:12095676). Is a potent regulator of the RB1 pathway through induction of RB1 expression (PubMed:14533007). Plays a crucial role in muscular differentiation (PubMed:12163359). Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis (By similarity).[UniProtKB:Q9ESK9]<ref>PMID:10769033</ref> <ref>PMID:12095676</ref> <ref>PMID:12163359</ref> <ref>PMID:12221124</ref> <ref>PMID:14533007</ref> <ref>PMID:21775823</ref> <ref>PMID:23392225</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The recruitment of Unc-51-like kinase and TANK-binding kinase 1 complexes is essential for Nuclear dot protein 52-mediated selective autophagy and relies on the specific association of NDP52, RB1-inducible coiled-coil protein 1, and Nak-associated protein 1 (5-azacytidine-induced protein 2, AZI2). However, the underlying molecular mechanism remains elusive. Here, we find that except for the NDP52 SKIP carboxyl homology (SKICH)/RB1CC1 coiled-coil interaction, the LC3-interacting region of NDP52 can directly interact with the RB1CC1 Claw domain, as that of NAP1 FIP200-binding region (FIR). The determined crystal structures of NDP52 SKICH/RB1CC1 complex, NAP1 FIR/RB1CC1 complex, and the related NAP1 FIR/Gamma-aminobutyric acid receptor-associated protein complex not only elucidate the molecular bases underpinning the interactions of RB1CC1 with NDP52 and NAP1 but also reveal that RB1CC1 Claw and Autophagy-related protein 8 family proteins are competitive in binding to NAP1 and NDP52. Overall, our findings provide mechanistic insights into the interactions of NDP52, NAP1 with RB1CC1 and ATG8 family proteins. | ||
| + | |||
| + | Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.,Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L Sci Adv. 2021 Aug 13;7(33). pii: 7/33/eabi6582. doi: 10.1126/sciadv.abi6582., Print 2021 Aug. PMID:34389544<ref>PMID:34389544</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7eaa" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Fu T]] |
| + | [[Category: Pan L]] | ||
Current revision
crystal structure of NDP52 SKICH domain in complex with RB1CC1 coiled-coil domain
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