2ktr

From Proteopedia

(Difference between revisions)

Revision as of 07:35, 29 April 2020

NMR structure of p62 PB1 dimer determined based on PCS

Structural highlights

2ktr is a 2 chain structure with sequence from Buffalo rat. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2kkc, 2rpv
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ktr"

@@ Line 1: / Line 1: @@
 ==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]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == 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 [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://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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kkc|2kkc]], [[2rpv|2rpv]]</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'>[http://proteopedia.org/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>
 </table>
 == Function ==
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Buffalo rat]]
+[[Category: Large Structures]]
 [[Category: Inagaki, F]]
 [[Category: Kumeta, H]]

2ktr

From Proteopedia

Revision as of 07:35, 29 April 2020

NMR structure of p62 PB1 dimer determined based on PCS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox