3v3l

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[[Image:3v3l.jpg|left|200px]]
 
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{{STRUCTURE_3v3l| PDB=3v3l | SCENE= }}
{{STRUCTURE_3v3l| PDB=3v3l | SCENE= }}
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===Crystal structure of human RNF146 WWE domain in complex with iso-ADPRibose===
===Crystal structure of human RNF146 WWE domain in complex with iso-ADPRibose===
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{{ABSTRACT_PUBMED_22267412}}
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==Disease==
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[[http://www.uniprot.org/uniprot/RN146_HUMAN RN146_HUMAN]] Note=Defects in RNF146 are a cause of susceptibility to breast cancer.
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==Function==
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[[http://www.uniprot.org/uniprot/RN146_HUMAN RN146_HUMAN]] E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair.<ref>PMID:21478859</ref><ref>PMID:21602803</ref><ref>PMID:21799911</ref><ref>PMID:21825151</ref><ref>PMID:22267412</ref>
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(as it appears on PubMed at http://www.pubmed.gov), where 22267412 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22267412}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:022267412</ref><references group="xtra"/>
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<ref group="xtra">PMID:022267412</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Cheng, Z.]]
[[Category: Cheng, Z.]]

Revision as of 01:09, 25 March 2013

Template:STRUCTURE 3v3l

Contents

Crystal structure of human RNF146 WWE domain in complex with iso-ADPRibose

Template:ABSTRACT PUBMED 22267412

Disease

[RN146_HUMAN] Note=Defects in RNF146 are a cause of susceptibility to breast cancer.

Function

[RN146_HUMAN] E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair.[1][2][3][4][5]

About this Structure

3v3l is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Wang Z, Michaud GA, Cheng Z, Zhang Y, Hinds TR, Fan E, Cong F, Xu W. Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination. Genes Dev. 2012 Feb 1;26(3):235-40. Epub 2012 Jan 19. PMID:22267412 doi:10.1101/gad.182618.111
  1. ↑ Zhang Y, Liu S, Mickanin C, Feng Y, Charlat O, Michaud GA, Schirle M, Shi X, Hild M, Bauer A, Myer VE, Finan PM, Porter JA, Huang SM, Cong F. RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling. Nat Cell Biol. 2011 May;13(5):623-9. doi: 10.1038/ncb2222. Epub 2011 Apr 10. PMID:21478859 doi:10.1038/ncb2222
  2. ↑ Andrabi SA, Kang HC, Haince JF, Lee YI, Zhang J, Chi Z, West AB, Koehler RC, Poirier GG, Dawson TM, Dawson VL. Iduna protects the brain from glutamate excitotoxicity and stroke by interfering with poly(ADP-ribose) polymer-induced cell death. Nat Med. 2011 Jun;17(6):692-9. doi: 10.1038/nm.2387. Epub 2011 May 22. PMID:21602803 doi:10.1038/nm.2387
  3. ↑ Callow MG, Tran H, Phu L, Lau T, Lee J, Sandoval WN, Liu PS, Bheddah S, Tao J, Lill JR, Hongo JA, Davis D, Kirkpatrick DS, Polakis P, Costa M. Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling. PLoS One. 2011;6(7):e22595. doi: 10.1371/journal.pone.0022595. Epub 2011 Jul 25. PMID:21799911 doi:10.1371/journal.pone.0022595
  4. ↑ Kang HC, Lee YI, Shin JH, Andrabi SA, Chi Z, Gagne JP, Lee Y, Ko HS, Lee BD, Poirier GG, Dawson VL, Dawson TM. Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage. Proc Natl Acad Sci U S A. 2011 Aug 23;108(34):14103-8. doi:, 10.1073/pnas.1108799108. Epub 2011 Aug 8. PMID:21825151 doi:10.1073/pnas.1108799108
  5. ↑ Wang Z, Michaud GA, Cheng Z, Zhang Y, Hinds TR, Fan E, Cong F, Xu W. Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination. Genes Dev. 2012 Feb 1;26(3):235-40. Epub 2012 Jan 19. PMID:22267412 doi:10.1101/gad.182618.111

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