2PE8

Crystal structure of the UHM domain of human SPF45 (free form)

2PE8 の概要

• エントリーDOI: 10.2210/pdb2pe8/pdb
• 分子名称: Splicing factor 45 (2 entities in total)
• 機能のキーワード: rrm, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q96I25
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11690.48

構造登録者

Corsini, L.,Basquin, J.,Hothorn, M.,Sattler, M. (登録日: 2007-04-02, 公開日: 2007-06-26, 最終更新日: 2023-08-30)

主引用文献

Corsini, L.,Bonna, S.,Basquin, J.,Hothorn, M.,Scheffzek, K.,Valcarcel, J.,Sattler, M.
U2AF-homology motif interactions are required for alternative splicing regulation by SPF45.
Nat.Struct.Mol.Biol., 14:620-629, 2007

PubMed Abstract: The U2AF-homology motif (UHM) mediates protein-protein interactions between factors involved in constitutive RNA splicing. Here we report that the splicing factor SPF45 regulates alternative splicing of the apoptosis regulatory gene FAS (also called CD95). The SPF45 UHM is necessary for this activity and binds UHM-ligand motifs (ULMs) present in the 3' splice site-recognizing factors U2AF65, SF1 and SF3b155. We describe a 2.1-A crystal structure of SPF45-UHM in complex with a ULM peptide from SF3b155. Features distinct from those of previously described UHM-ULM structures allowed the design of mutations in the SPF45 UHM that selectively impair binding to individual ULMs. Splicing assays using the ULM-selective SPF45 variants demonstrate that individual UHM-ULM interactions are required for FAS splicing regulation by SPF45 in vivo. Our data suggest that networks of UHM-ULM interactions are involved in regulating alternative splicing.

PubMed: 17589525
DOI: 10.1038/nsmb1260

実験手法

X-RAY DIFFRACTION (2 Å)