7EVS

Crystal structure of hnRNP LL RRM2 in complex with SETD2

7EVS の概要

• エントリーDOI: 10.2210/pdb7evs/pdb
• 分子名称: Heterogeneous nuclear ribonucleoprotein L-like, SHI domain from Histone-lysine N-methyltransferase SETD2, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: complex, rna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 28056.40

構造登録者

Li, F.D.,Wang, S.M. (登録日: 2021-05-22, 公開日: 2021-10-20, 最終更新日: 2023-11-29)

主引用文献

Bhattacharya, S.,Wang, S.,Reddy, D.,Shen, S.,Zhang, Y.,Zhang, N.,Li, H.,Washburn, M.P.,Florens, L.,Shi, Y.,Workman, J.L.,Li, F.
Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing.
Nat Commun, 12:6452-6452, 2021

PubMed Abstract: The RNA recognition motif (RRM) binds to nucleic acids as well as proteins. More than one such domain is found in the pre-mRNA processing hnRNP proteins. While the mode of RNA recognition by RRMs is known, the molecular basis of their protein interaction remains obscure. Here we describe the mode of interaction between hnRNP L and LL with the methyltransferase SETD2. We demonstrate that for the interaction to occur, a leucine pair within a highly conserved stretch of SETD2 insert their side chains in hydrophobic pockets formed by hnRNP L RRM2. Notably, the structure also highlights that RRM2 can form a ternary complex with SETD2 and RNA. Remarkably, mutating the leucine pair in SETD2 also results in its reduced interaction with other hnRNPs. Importantly, the similarity that the mode of SETD2-hnRNP L interaction shares with other related protein-protein interactions reveals a conserved design by which splicing regulators interact with one another.

PubMed: 34750379
DOI: 10.1038/s41467-021-26799-3

実験手法

X-RAY DIFFRACTION (1.6 Å)