4QPT

Structural Investigation of hnRNP L

4QPT の概要

• エントリーDOI: 10.2210/pdb4qpt/pdb
• 関連するPDBエントリー: 2mql 2mqm 2mqo
• 分子名称: Heterogenous nuclear ribonucleoprotein L, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: rna recognition motif, rrm, rna, rna binding protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24236.24

構造登録者

Blatter, M.,Allain, F.H.-T. (登録日: 2014-06-25, 公開日: 2015-05-20, 最終更新日: 2024-02-28)

主引用文献

Blatter, M.,Dunin-Horkawicz, S.,Grishina, I.,Maris, C.,Thore, S.,Maier, T.,Bindereif, A.,Bujnicki, J.M.,Allain, F.H.
The Signature of the Five-Stranded vRRM Fold Defined by Functional, Structural and Computational Analysis of the hnRNP L Protein.
J.Mol.Biol., 427:3001-3022, 2015

PubMed Abstract: The RNA recognition motif (RRM) is the far most abundant RNA binding domain. In addition to the typical β1α1β2β3α2β4 fold, various sub-structural elements have been described and reportedly contribute to the high functional versatility of RRMs. The heterogeneous nuclear ribonucleoprotein L (hnRNP L) is a highly abundant protein of 64 kDa comprising four RRM domains. Involved in many aspects of RNA metabolism, hnRNP L specifically binds to RNAs containing CA repeats or CA-rich clusters. However, a comprehensive structural description of hnRNP L including its sub-structural elements is missing. Here, we present the structural characterization of the RRM domains of hnRNP L and demonstrate their function in repressing exon 4 of SLC2A2. By comparison of the sub-structural elements between the two highly similar paralog families of hnRNP L and PTB, we defined signatures underlying interacting C-terminal coils (ICCs), the RRM34 domain interaction and RRMs with a C-terminal fifth β-strand, a variation we denoted vRRMs. Furthermore, computational analysis revealed new putative ICC-containing RRM families and allowed us to propose an evolutionary scenario explaining the origins of the ICC and fifth β-strand sub-structural extensions. Our studies provide insights of domain requirements in alternative splicing mediated by hnRNP L and molecular descriptions for the sub-structural elements. In addition, the analysis presented may help to classify other abundant RRM extensions and to predict structure-function relationships.

PubMed: 26051023
DOI: 10.1016/j.jmb.2015.05.020

実験手法

X-RAY DIFFRACTION (1.351 Å)