1HD0

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0 (HNRNP D0 RBD1), NMR

1HD0 の概要

• エントリーDOI: 10.2210/pdb1hd0/pdb
• 関連するPDBエントリー: 1HD1
• 分子名称: PROTEIN (HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0) (1 entity in total)
• 機能のキーワード: 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: 8572.93

構造登録者

Nagata, T.,Kurihara, Y.,Matsuda, G.,Saeki, J.,Kohno, T.,Yanagida, Y.,Ishikawa, F.,Uesugi, S.,Katahira, M. (登録日: 1999-05-18, 公開日: 2000-05-18, 最終更新日: 2023-12-27)

主引用文献

Nagata, T.,Kurihara, Y.,Matsuda, G.,Saeki, J.,Kohno, T.,Yanagida, Y.,Ishikawa, F.,Uesugi, S.,Katahira, M.
Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0.
J.Mol.Biol., 287:221-237, 1999

PubMed Abstract: Heterogeneous nuclear ribonucleoprotein (hnRNP) D0 has two ribonucleoprotein (RNP)-type RNA-binding domains (RBDs), each of which can bind solely to the UUAG sequence specifically. The structure of the N-terminal RBD (RBD1) determined by NMR is presented here. It folds into a compact alphabeta structure comprising a four-stranded antiparallel beta-sheet packed against two alpha-helices, which is characteristic of the RNP-type RBDs. Special structural features of RBD1 include N-capping boxes for both alpha-helices, a beta-bulge in the second beta-strand, and an additional short antiparallel beta-sheet coupled with a beta-turn-like structure in a loop. Two hydrogen bonds which restrict the positions of loops were identified. Backbone resonance assignments for RBD1 complexed with r(UUAGGG) revealed that the overall folding is maintained in the complex. The candidate residues involved in the interactions with RNA were identified by chemical shift perturbation analysis. They are located in the central and peripheral regions of the RNA-binding surface composed of the four-stranded beta-sheet, loops, and the C-terminal region. It is suggested that non-specific interactions with RNA are performed by the residues in the central region of the RNA-binding surface, while specific interactions are performed by those in the peripheral regions. It was also found that RBD1 has the ability to inhibit the formation of the quadruplex structure.

PubMed: 10080887
DOI: 10.1006/jmbi.1999.2616

実験手法

SOLUTION NMR