7JYN

Solution NMR structure of human Brd3 ET complexed with NSD3(148-184) peptide

7JYN の概要

• エントリーDOI: 10.2210/pdb7jyn/pdb
• NMR情報: BMRB: 30790
• 分子名称: Bromodomain-containing protein 3, Histone-lysine N-methyltransferase NSD3 (2 entities in total)
• 機能のキーワード: brd3 et, nsd3 solution nmr, integrase, extra terminal domain, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15594.38

構造登録者

Aiyer, S.,Swapna, G.V.T.,Roth, M.J.,Montelione, G.T. (登録日: 2020-08-31, 公開日: 2021-06-23, 最終更新日: 2024-05-15)

主引用文献

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

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

実験手法

SOLUTION NMR