2N1D

Solution structure of the MRG15-MRGBP complex


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 80 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy, restraint violations, and RMS deviations from the ideal covalent geometry 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Basis for Multi-specificity of MRG Domains.

Xie, T.Zmyslowski, A.M.Zhang, Y.Radhakrishnan, I.

(2015) Structure 23: 1049-1057

  • DOI: https://doi.org/10.1016/j.str.2015.03.020
  • Primary Citation of Related Structures:  
    2N1D

  • PubMed Abstract: 

    Chromatin-binding proteins play vital roles in the assembly and recruitment of multi-subunit complexes harboring effector proteins to specific genomic loci. MRG15, a chromodomain-containing chromatin-binding protein, recruits diverse chromatin-associated complexes that regulate gene transcription, DNA repair, and RNA splicing. Previous studies with Pf1, another chromatin-binding subunit of the Sin3S/Rpd3S histone deacetylase complex, defined the sequence and structural requirements for interactions with the MRG15 MRG domain, a common target of diverse subunits in the aforementioned complexes. We now show that MRGBP, a member of the Tip60/NuA4 histone acetyltransferase complex, engages the same two surfaces of the MRG domain as Pf1. High-affinity interactions occur via a bipartite structural motif including an FxLP sequence motif. MRGBP shares little sequence and structural similarity with Pf1, yet targets similar pockets on the surface of the MRG domain, mimicking Pf1 in its interactions. Our studies shed light onto how MRG domains have evolved to bind diverse targets.


  • Organizational Affiliation

    Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MRG/MORF4L-binding protein54Homo sapiensMutation(s): 0 
Gene Names: MRGBPC20orf20
UniProt & NIH Common Fund Data Resources
Find proteins for Q9NV56 (Homo sapiens)
Explore Q9NV56 
Go to UniProtKB:  Q9NV56
PHAROS:  Q9NV56
GTEx:  ENSG00000101189 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9NV56
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Mortality factor 4-like protein 1172Homo sapiensMutation(s): 0 
Gene Names: MORF4L1MRG15FWP006HSPC008HSPC061PP368
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UBU8 (Homo sapiens)
Explore Q9UBU8 
Go to UniProtKB:  Q9UBU8
PHAROS:  Q9UBU8
GTEx:  ENSG00000185787 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9UBU8
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 80 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy, restraint violations, and RMS deviations from the ideal covalent geometry 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-05-27
    Type: Initial release
  • Version 1.1: 2015-06-17
    Changes: Database references
  • Version 1.2: 2023-06-14
    Changes: Data collection, Database references, Other
  • Version 1.3: 2024-05-15
    Changes: Data collection, Database references