3nw0

From Proteopedia

(Difference between revisions)

Revision as of 04:56, 25 December 2014

Crystal structure of MAGEG1 and NSE1 complex

Structural highlights

3nw0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	HCA4, MAGEG1, NDNL2, NSMCE1 (Homo sapiens), HSPC333, HSPC337, NDNL2, NSMCE1 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[MAGG1_HUMAN] Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest.^[1] [NSE1_HUMAN] Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Has in vitro ubiquitin ligase activity in presence of NDNL2. Is involved in positive regulation of response to DNA damage stimulus.^[2] ^[3]

Publication Abstract from PubMed

The melanoma antigen (MAGE) family consists of more than 60 genes, many of which are cancer-testis antigens that are highly expressed in cancer and play a critical role in tumorigenesis. However, the biochemical and cellular functions of this enigmatic family of proteins have remained elusive. Here, we identify really interesting new gene (RING) domain proteins as binding partners for MAGE family proteins. Multiple MAGE family proteins bind E3 RING ubiquitin ligases with specificity. The crystal structure of one of these MAGE-RING complexes, MAGE-G1-NSE1, reveals structural insights into MAGE family proteins and their interaction with E3 RING ubiquitin ligases. Biochemical and cellular assays demonstrate that MAGE proteins enhance the ubiquitin ligase activity of RING domain proteins. For example, MAGE-C2-TRIM28 is shown to target p53 for degradation in a proteasome-dependent manner, consistent with its tumorigenic functions. These findings define a biochemical and cellular function for the MAGE protein family.

MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.,Doyle JM, Gao J, Wang J, Yang M, Potts PR Mol Cell. 2010 Sep 24;39(6):963-74. PMID:20864041^[4]

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

References

↑ Doyle JM, Gao J, Wang J, Yang M, Potts PR. MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases. Mol Cell. 2010 Sep 24;39(6):963-74. PMID:20864041 doi:10.1016/j.molcel.2010.08.029
↑ Taylor EM, Copsey AC, Hudson JJ, Vidot S, Lehmann AR. Identification of the proteins, including MAGEG1, that make up the human SMC5-6 protein complex. Mol Cell Biol. 2008 Feb;28(4):1197-206. Epub 2007 Dec 17. PMID:18086888 doi:10.1128/MCB.00767-07
↑ Doyle JM, Gao J, Wang J, Yang M, Potts PR. MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases. Mol Cell. 2010 Sep 24;39(6):963-74. PMID:20864041 doi:10.1016/j.molcel.2010.08.029
↑ Doyle JM, Gao J, Wang J, Yang M, Potts PR. MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases. Mol Cell. 2010 Sep 24;39(6):963-74. PMID:20864041 doi:10.1016/j.molcel.2010.08.029

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3nw0"

@@ Line 7: / Line 7: @@
 <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=3nw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nw0 RCSB], [http://www.ebi.ac.uk/pdbsum/3nw0 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MAGG1_HUMAN MAGG1_HUMAN]] Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). In vitro enhances ubiquitin ligase activity of NSMCE1. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May be a growth suppressor that facilitates the entry of the cell into cell cycle arrest.<ref>PMID:20864041</ref>  [[http://www.uniprot.org/uniprot/NSE1_HUMAN NSE1_HUMAN]] Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Has in vitro ubiquitin ligase activity in presence of NDNL2. Is involved in positive regulation of response to DNA damage stimulus.<ref>PMID:18086888</ref> <ref>PMID:20864041</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3nw0

From Proteopedia

Revision as of 04:56, 25 December 2014

Crystal structure of MAGEG1 and NSE1 complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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