5WY5

Crystal structure of MAGEG1 and NSE1 complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.92 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.219 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Mage-Ring Protein Complexes Comprise A Family Of E3 Ubiquitin Ligases.

Doyle, J.M.Gao, J.Wang, J.Yang, M.Potts, P.R.

(2010) Mol Cell 39: 963-974

  • DOI: https://doi.org/10.1016/j.molcel.2010.08.029
  • Primary Citation of Related Structures:  
    5WY5

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390-9038, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Melanoma-associated antigen G1A [auth B]217Homo sapiensMutation(s): 2 
Gene Names: NSMCE3HCA4MAGEG1NDNL2
UniProt & NIH Common Fund Data Resources
Find proteins for Q96MG7 (Homo sapiens)
Explore Q96MG7 
Go to UniProtKB:  Q96MG7
PHAROS:  Q96MG7
GTEx:  ENSG00000185115 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ96MG7
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Non-structural maintenance of chromosomes element 1 homologB [auth A]238Homo sapiensMutation(s): 0 
Gene Names: NSMCE1HSPC333HSPC337
EC: 6.3.2
UniProt & NIH Common Fund Data Resources
Find proteins for Q8WV22 (Homo sapiens)
Explore Q8WV22 
Go to UniProtKB:  Q8WV22
PHAROS:  Q8WV22
GTEx:  ENSG00000169189 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8WV22
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.92 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.216 
  • R-Value Observed: 0.219 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.257α = 90
b = 154.327β = 90
c = 53.726γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASESphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data

  • Released Date: 2017-05-03 
  • Deposition Author(s): Yang, M., Gao, J.
  • This entry supersedes: 3NW0

Funding OrganizationLocationGrant Number
Tsinghua University Startup FundsChinaM.Y.
National Natural Science Foundation of ChinaChinaSpecial Fund 2060204
Sara and Frank McKnight FellowshipUnited StatesP.R.P.

Revision History  (Full details and data files)

  • Version 1.0: 2017-05-03
    Type: Initial release
  • Version 1.1: 2017-10-04
    Changes: Data collection
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references