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| | ==NMR structure of p62 PB1 dimer determined based on PCS== | | ==NMR structure of p62 PB1 dimer determined based on PCS== |
| - | <StructureSection load='2ktr' size='340' side='right' caption='[[2ktr]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2ktr' size='340' side='right'caption='[[2ktr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ktr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KTR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ktr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KTR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kkc|2kkc]], [[2rpv|2rpv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</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=2ktr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktr OCA], [http://pdbe.org/2ktr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ktr RCSB], [http://www.ebi.ac.uk/pdbsum/2ktr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ktr 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=2ktr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktr OCA], [https://pdbe.org/2ktr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ktr RCSB], [https://www.ebi.ac.uk/pdbsum/2ktr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ktr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SQSTM_RAT SQSTM_RAT]] Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures). Links ALIS to the autophagic machinery via direct interaction with MAP1 LC3 family members (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Isoform 1 is more potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2.<ref>PMID:10477520</ref> <ref>PMID:11244088</ref> <ref>PMID:11500922</ref> | + | [https://www.uniprot.org/uniprot/SQSTM_RAT SQSTM_RAT] Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures). Links ALIS to the autophagic machinery via direct interaction with MAP1 LC3 family members (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Isoform 1 is more potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2.<ref>PMID:10477520</ref> <ref>PMID:11244088</ref> <ref>PMID:11500922</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Inagaki, F]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Kumeta, H]] | + | [[Category: Inagaki F]] |
| - | [[Category: Saio, T]] | + | [[Category: Kumeta H]] |
| - | [[Category: Yokochi, M]] | + | [[Category: Saio T]] |
| - | [[Category: Autophagy]]
| + | [[Category: Yokochi M]] |
| - | [[Category: Homo-oligomer]]
| + | |
| - | [[Category: Nf-kb signaling]]
| + | |
| - | [[Category: Pb1 dimer]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
SQSTM_RAT Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures). Links ALIS to the autophagic machinery via direct interaction with MAP1 LC3 family members (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Isoform 1 is more potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A simple and fast nuclear magnetic resonance method for docking proteins using pseudo-contact shift (PCS) and (1)H(N)/(15)N chemical shift perturbation is presented. PCS is induced by a paramagnetic lanthanide ion that is attached to a target protein using a lanthanide binding peptide tag anchored at two points. PCS provides long-range (approximately 40 A) distance and angular restraints between the lanthanide ion and the observed nuclei, while the (1)H(N)/(15)N chemical shift perturbation data provide loose contact-surface information. The usefulness of this method was demonstrated through the structure determination of the p62 PB1-PB1 complex, which forms a front-to-back 20 kDa homo-oligomer. As p62 PB1 does not intrinsically bind metal ions, the lanthanide binding peptide tag was attached to one subunit of the dimer at two anchoring points. Each monomer was treated as a rigid body and was docked based on the backbone PCS and backbone chemical shift perturbation data. Unlike NOE-based structural determination, this method only requires resonance assignments of the backbone (1)H(N)/(15)N signals and the PCS data obtained from several sets of two-dimensional (15)N-heteronuclear single quantum coherence spectra, thus facilitating rapid structure determination of the protein-protein complex.
PCS-based structure determination of protein-protein complexes.,Saio T, Yokochi M, Kumeta H, Inagaki F J Biomol NMR. 2010 Apr;46(4):271-80. Epub 2010 Mar 19. PMID:20300805[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gong J, Xu J, Bezanilla M, van Huizen R, Derin R, Li M. Differential stimulation of PKC phosphorylation of potassium channels by ZIP1 and ZIP2. Science. 1999 Sep 3;285(5433):1565-9. PMID:10477520
- ↑ Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J. The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. J Biol Chem. 2001 Mar 16;276(11):7709-12. Epub 2001 Jan 22. PMID:11244088 doi:10.1074/jbc.C000869200
- ↑ Samuels IS, Seibenhener ML, Neidigh KB, Wooten MW. Nerve growth factor stimulates the interaction of ZIP/p62 with atypical protein kinase C and targets endosomal localization: evidence for regulation of nerve growth factor-induced differentiation. J Cell Biochem. 2001;82(3):452-66. PMID:11500922
- ↑ Saio T, Yokochi M, Kumeta H, Inagaki F. PCS-based structure determination of protein-protein complexes. J Biomol NMR. 2010 Apr;46(4):271-80. Epub 2010 Mar 19. PMID:20300805 doi:10.1007/s10858-010-9401-4
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