2N1D

Solution structure of the MRG15-MRGBP complex

Summary for 2N1D

• Entry DOI: 10.2210/pdb2n1d/pdb
• Related: 2LKM
• NMR Information: BMRB: 25556
• Descriptor: MRG/MORF4L-binding protein, Mortality factor 4-like protein 1 (2 entities in total)
• Functional Keywords: mrg domain, protein-protein interaction, tip60-nua4 complex, hat complex, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9NV56 Q9UBU8
• Total number of polymer chains: 2
• Total formula weight: 26126.78

Authors

Xie, T.,Zmysloski, A.M.,Zhang, Y.,Radhakrishnan, I. (deposition date: 2015-03-27, release date: 2015-05-27, Last modification date: 2024-05-15)

Primary citation

Xie, T.,Zmyslowski, A.M.,Zhang, Y.,Radhakrishnan, I.
Structural Basis for Multi-specificity of MRG Domains.
Structure, 23:1049-1057, 2015

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.

PubMed: 25960410
DOI: 10.1016/j.str.2015.03.020

Experimental method

SOLUTION NMR