2HH3

Solution structure of the third KH domain of KSRP

2HH3 の概要

• エントリーDOI: 10.2210/pdb2hh3/pdb
• 関連するPDBエントリー: 2HH2
• 分子名称: KH-type splicing regulatory protein (1 entity in total)
• 機能のキーワード: kh-rna binding domain, rna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10850.40

構造登録者

Garcia-Mayoral, M.F. (登録日: 2006-06-27, 公開日: 2007-05-08, 最終更新日: 2024-05-29)

主引用文献

Garcia-Mayoral, M.F.,Hollingworth, D.,Masino, L.,Diaz-Moreno, I.,Kelly, G.,Gherzi, R.,Chou, C.F.,Chen, C.Y.,Ramos, A.
The Structure of the C-Terminal KH Domains of KSRP Reveals a Noncanonical Motif Important for mRNA Degradation.
Structure, 15:485-498, 2007

PubMed Abstract: The AU-rich element (ARE) RNA-binding protein KSRP (K-homology splicing regulator protein) contains four KH domains and promotes the degradation of specific mRNAs that encode proteins with functions in cellular proliferation and inflammatory response. The fourth KH domain (KH4) is essential for mRNA recognition and decay but requires the third KH domain (KH3) for its function. We show that KH3 and KH4 behave as independent binding modules and can interact with different regions of the AU-rich RNA targets of KSRP. This provides KSRP with the structural flexibility needed to recognize a set of different targets in the context of their 3'UTR structural settings. Surprisingly, we find that KH4 binds to its target AREs with lower affinity than KH3 and that KSRP's mRNA binding, and mRNA degradation activities are closely associated with a conserved structural element of KH4.

PubMed: 17437720
DOI: 10.1016/j.str.2007.03.006

実験手法

SOLUTION NMR