2l8j

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[[Image:2l8j.png|left|200px]]
 
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{{STRUCTURE_2l8j| PDB=2l8j | SCENE= }}
{{STRUCTURE_2l8j| PDB=2l8j | SCENE= }}
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===GABARAPL-1 NBR1-LIR complex structure===
===GABARAPL-1 NBR1-LIR complex structure===
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{{ABSTRACT_PUBMED_21620860}}
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==Function==
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[[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>
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{{ABSTRACT_PUBMED_21620860}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:021620860</ref><references group="xtra"/>
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<ref group="xtra">PMID:021620860</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Dikic, I.]]
[[Category: Dikic, I.]]

Revision as of 08:18, 8 May 2013

Template:STRUCTURE 2l8j

Contents

GABARAPL-1 NBR1-LIR complex structure

Template:ABSTRACT PUBMED 21620860

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]

About this Structure

2l8j is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • 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. 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
  2. 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
  3. 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

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