5ypg: Difference between revisions
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==Zinc binding protein complexed with Leu-peptide== | |||
<StructureSection load='5ypg' size='340' side='right' caption='[[5ypg]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ypg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YPG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5ypg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ypg OCA], [http://pdbe.org/5ypg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ypg RCSB], [http://www.ebi.ac.uk/pdbsum/5ypg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ypg ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Note=Autoantigen in rheumatoid arthritis.<ref>PMID:11160188</ref> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.<ref>PMID:2294010</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
p62/SQSTM1 is the key autophagy adapter protein and the hub of multi-cellular signaling. It was recently reported that autophagy and N-end rule pathways are linked via p62. However, the exact recognition mode of degrading substrates and regulation of p62 in the autophagic pathway remain unknown. Here, we present the complex structures between the ZZ-domain of p62 and various type-1 and type-2 N-degrons. The binding mode employed in the interaction of the ZZ-domain with N-degrons differs from that employed by classic N-recognins. It was also determined that oligomerization via the PB1 domain can control functional affinity to the R-BiP substrate. Unexpectedly, we found that self-oligomerization and disassembly of p62 are pH-dependent. These findings broaden our understanding of the functional repertoire of the N-end rule pathway and provide an insight into the regulation of p62 during the autophagic pathway. | |||
Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter.,Kwon DH, Park OH, Kim L, Jung YO, Park Y, Jeong H, Hyun J, Kim YK, Song HK Nat Commun. 2018 Aug 17;9(1):3291. doi: 10.1038/s41467-018-05825-x. PMID:30120248<ref>PMID:30120248</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ypg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kim, L]] | [[Category: Kim, L]] | ||
[[Category: Song, H | [[Category: Kwon, D H]] | ||
[[Category: Song, H K]] | |||
[[Category: Autophagy]] | |||
[[Category: Complex]] | |||
[[Category: N-end rule]] | |||
[[Category: P62/sqstm1]] | |||
[[Category: Signaling protein]] | |||
[[Category: Zz domain]] | |||
Revision as of 10:19, 29 August 2018
Zinc binding protein complexed with Leu-peptideZinc binding protein complexed with Leu-peptide
Structural highlights
Disease[GRP78_HUMAN] Note=Autoantigen in rheumatoid arthritis.[1] Function[GRP78_HUMAN] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.[2] Publication Abstract from PubMedp62/SQSTM1 is the key autophagy adapter protein and the hub of multi-cellular signaling. It was recently reported that autophagy and N-end rule pathways are linked via p62. However, the exact recognition mode of degrading substrates and regulation of p62 in the autophagic pathway remain unknown. Here, we present the complex structures between the ZZ-domain of p62 and various type-1 and type-2 N-degrons. The binding mode employed in the interaction of the ZZ-domain with N-degrons differs from that employed by classic N-recognins. It was also determined that oligomerization via the PB1 domain can control functional affinity to the R-BiP substrate. Unexpectedly, we found that self-oligomerization and disassembly of p62 are pH-dependent. These findings broaden our understanding of the functional repertoire of the N-end rule pathway and provide an insight into the regulation of p62 during the autophagic pathway. Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter.,Kwon DH, Park OH, Kim L, Jung YO, Park Y, Jeong H, Hyun J, Kim YK, Song HK Nat Commun. 2018 Aug 17;9(1):3291. doi: 10.1038/s41467-018-05825-x. PMID:30120248[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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