7czg
From Proteopedia
(Difference between revisions)
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==Crystal structure of FIP200 Claw domain apo form== | ==Crystal structure of FIP200 Claw domain apo form== | ||
| - | <StructureSection load='7czg' size='340' side='right'caption='[[7czg]]' scene=''> | + | <StructureSection load='7czg' size='340' side='right'caption='[[7czg]], [[Resolution|resolution]] 1.80Å' 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=7CZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CZG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7czg]] 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=7CZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CZG 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=7czg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7czg OCA], [https://pdbe.org/7czg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7czg RCSB], [https://www.ebi.ac.uk/pdbsum/7czg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7czg 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]] 1.8Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=7czg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7czg OCA], [https://pdbe.org/7czg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7czg RCSB], [https://www.ebi.ac.uk/pdbsum/7czg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7czg 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 ULK complex initiates the autophagosome formation, and has recently been implicated in selective autophagy by interacting with autophagy receptors through its FIP200 subunit. However, the structural mechanism underlying the interactions of autophagy receptors with FIP200 and the relevant regulatory mechanism remain elusive. Here, we discover that the interactions of FIP200 Claw domain with autophagy receptors CCPG1 and Optineurin can be regulated by the phosphorylation in their respective FIP200-binding regions. We determine the crystal structures of FIP200 Claw in complex with the phosphorylated CCPG1 and Optineurin, and elucidate the detailed molecular mechanism governing the interactions of FIP200 Claw with CCPG1 and Optineurin as well as their potential regulations by kinase-mediated phosphorylation. In addition, we define the consensus FIP200 Claw-binding motif, and find other autophagy receptors that contain this motif within their conventional LC3-interacting regions. In all, our findings uncover a general and phosphoregulatable binding mode shared by many autophagy receptors to interact with FIP200 Claw for autophagosome biogenesis, and are valuable for further understanding the molecular mechanism of selective autophagy. | ||
| + | |||
| + | Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation.,Zhou Z, Liu J, Fu T, Wu P, Peng C, Gong X, Wang Y, Zhang M, Li Y, Wang Y, Xu X, Li M, Pan L Nat Commun. 2021 Mar 10;12(1):1570. doi: 10.1038/s41467-021-21874-1. PMID:33692357<ref>PMID:33692357</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7czg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pan LF]] | [[Category: Pan LF]] | ||
[[Category: Zhou ZX]] | [[Category: Zhou ZX]] | ||
Current revision
Crystal structure of FIP200 Claw domain apo form
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