This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2l8j

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:38, 14 April 2021

GABARAPL-1 NBR1-LIR complex structure

Structural highlights

2l8j is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	GABARAPL1, GEC1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GBRL1_HUMAN] Increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles.^[1] ^[2] [NBR1_HUMAN] Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets.^[3]

Publication Abstract from PubMed

Selective autophagy requires the specific segregation of targeted proteins into autophagosomes. The selectivity is mediated by autophagy receptors, such as p62 and NBR1, which can bind to autophagic effector proteins (Atg8 in yeast, MAP1LC3 protein family in mammals) anchored in the membrane of autophagosomes. Recognition of autophagy receptors by autophagy effectors takes place through an LC3 interaction region (LIR). The canonical LIR motif consists of a WXXL sequence, N-terminally preceded by negatively charged residues. The LIR motif of NBR1 presents differences to this classical LIR motif with a tyrosine residue and an isoleucine residue substituting the tryptophan residue and the leucine residue, respectively. We have determined the structure of the GABARAPL-1/NBR1-LIR complex and studied the influence of the different residues belonging to the LIR motif for the interaction with several mammalian autophagy modifiers (LC3B and GABARAPL-1). Our results indicate that the presence of a tryptophan residue in the LIR motif increases the binding affinity. Substitution by other aromatic amino acids or increasing the number of negatively charged residues at the N-terminus of the LIR motif, however, has little effect on the binding affinity due to enthalpy-entropy compensation. This indicates that different LIRs can interact with autophagy modifiers with unique binding properties.

Characterization of the Interaction of GABARAPL-1 with the LIR Motif of NBR1.,Rozenknop A, Rogov VV, Rogova NY, Lohr F, Guntert P, Dikic I, Dotsch V J Mol Biol. 2011 Jul 15;410(3):477-87. Epub 2011 May 18. PMID:21620860^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chen C, Li JG, Chen Y, Huang P, Wang Y, Liu-Chen LY. GEC1 interacts with the kappa opioid receptor and enhances expression of the receptor. J Biol Chem. 2006 Mar 24;281(12):7983-93. Epub 2006 Jan 23. PMID:16431922 doi:M509805200
↑ Chakrama FZ, Seguin-Py S, Le Grand JN, Fraichard A, Delage-Mourroux R, Despouy G, Perez V, Jouvenot M, Boyer-Guittaut M. GABARAPL1 (GEC1) associates with autophagic vesicles. Autophagy. 2010 May;6(4):495-505. doi: 10.4161/auto.6.4.11819. Epub 2010 May 16. PMID:20404487 doi:10.4161/auto.6.4.11819
↑ Kirkin V, Lamark T, Sou YS, Bjorkoy G, Nunn JL, Bruun JA, Shvets E, McEwan DG, Clausen TH, Wild P, Bilusic I, Theurillat JP, Overvatn A, Ishii T, Elazar Z, Komatsu M, Dikic I, Johansen T. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell. 2009 Feb 27;33(4):505-16. doi: 10.1016/j.molcel.2009.01.020. PMID:19250911 doi:10.1016/j.molcel.2009.01.020
↑ Rozenknop A, Rogov VV, Rogova NY, Lohr F, Guntert P, Dikic I, Dotsch V. Characterization of the Interaction of GABARAPL-1 with the LIR Motif of NBR1. J Mol Biol. 2011 Jul 15;410(3):477-87. Epub 2011 May 18. PMID:21620860 doi:10.1016/j.jmb.2011.05.003

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l8j"

@@ Line 1: / Line 1: @@
 ==GABARAPL-1 NBR1-LIR complex structure==
-<StructureSection load='2l8j' size='340' side='right' caption='[[2l8j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l8j' size='340' side='right'caption='[[2l8j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l8j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L8J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l8j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L8J FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GABARAPL1, GEC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GABARAPL1, GEC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2l8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8j OCA], [http://pdbe.org/2l8j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l8j RCSB], [http://www.ebi.ac.uk/pdbsum/2l8j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l8j 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=2l8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8j OCA], [https://pdbe.org/2l8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l8j RCSB], [https://www.ebi.ac.uk/pdbsum/2l8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l8j ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GBRL1_HUMAN GBRL1_HUMAN]] Increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles.<ref>PMID:16431922</ref> <ref>PMID:20404487</ref>  [[http://www.uniprot.org/uniprot/NBR1_HUMAN NBR1_HUMAN]] Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets.<ref>PMID:19250911</ref>
+[[https://www.uniprot.org/uniprot/GBRL1_HUMAN GBRL1_HUMAN]] Increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles.<ref>PMID:16431922</ref> <ref>PMID:20404487</ref>  [[https://www.uniprot.org/uniprot/NBR1_HUMAN NBR1_HUMAN]] Acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets.<ref>PMID:19250911</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 20: @@
 ==See Also==
-*[[GABA(A) receptor-associated protein|GABA(A) receptor-associated protein]]
+*[[GABA receptor-associated protein 3D structures|GABA receptor-associated protein 3D structures]]
 == References ==
 <references/>
@@ Line 26: / Line 26: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Dikic, I]]
 [[Category: Doetsch, V]]

2l8j

From Proteopedia

Revision as of 07:38, 14 April 2021

GABARAPL-1 NBR1-LIR complex structure

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox