7JYN
Solution NMR structure of human Brd3 ET complexed with NSD3(148-184) peptide
Summary for 7JYN
| Entry DOI | 10.2210/pdb7jyn/pdb |
| NMR Information | BMRB: 30790 |
| Descriptor | Bromodomain-containing protein 3, Histone-lysine N-methyltransferase NSD3 (2 entities in total) |
| Functional Keywords | brd3 et, nsd3 solution nmr, integrase, extra terminal domain, signaling protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 15594.38 |
| Authors | Aiyer, S.,Swapna, G.V.T.,Roth, M.J.,Montelione, G.T. (deposition date: 2020-08-31, release date: 2021-06-23, Last modification date: 2024-05-15) |
| Primary citation | Aiyer, S.,Swapna, G.V.T.,Ma, L.C.,Liu, G.,Hao, J.,Chalmers, G.,Jacobs, B.C.,Montelione, G.T.,Roth, M.J. A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins. Structure, 29:886-898.e6, 2021 Cited by PubMed Abstract: The extraterminal (ET) domain of BRD3 is conserved among BET proteins (BRD2, BRD3, BRD4), interacting with multiple host and viral protein-protein networks. Solution NMR structures of complexes formed between the BRD3 ET domain and either the 79-residue murine leukemia virus integrase (IN) C-terminal domain (IN) or its 22-residue IN tail peptide (IN) alone reveal similar intermolecular three-stranded β-sheet formations. N relaxation studies reveal a 10-residue linker region (IN) tethering the SH3 domain (IN) to the ET-binding motif (IN):ET complex. This linker has restricted flexibility, affecting its potential range of orientations in the IN:nucleosome complex. The complex of the ET-binding peptide of the host NSD3 protein (NSD3) and the BRD3 ET domain includes a similar three-stranded β-sheet interaction, but the orientation of the β hairpin is flipped compared with the two IN:ET complexes. These studies expand our understanding of molecular recognition polymorphism in complexes of ET-binding motifs with viral and host proteins. PubMed: 33592170DOI: 10.1016/j.str.2021.01.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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