7JQ8

Solution NMR structure of human Brd3 ET domain

Summary for 7JQ8

• Entry DOI: 10.2210/pdb7jq8/pdb
• Related: 7JMY
• NMR Information: BMRB: 30786
• Descriptor: Bromodomain-containing protein 3, Integrase peptide (2 entities in total)
• Functional Keywords: bet proteins, brd3, extra-terminal domain, mlv-in tp, signaling protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 14076.82

Authors

Aiyer, S.,Swapna, G.V.T.,Roth, J.M.,Montelione, G.T. (deposition date: 2020-08-10, 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-, 2021

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: 33592170
DOI: 10.1016/j.str.2021.01.010

Experimental method

SOLUTION NMR