1X0F

Complex structure of the C-terminal RNA-binding domain of hnRNP D(AUF1) with telomeric DNA

1X0F の概要

• エントリーDOI: 10.2210/pdb1x0f/pdb
• 関連するPDBエントリー: 1HD0 1HD1 1IQT 1WTB
• 分子名称: 5'-D(P*TP*AP*GP*G)-3', Heterogeneous nuclear ribonucleoprotein D0 (2 entities in total)
• 機能のキーワード: rna-binding domain, dna-binding domain, rrm, hnrnp d, auf1, telomere, complex, structural genomics, transcription-dna complex, transcription/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q14103
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10334.48

構造登録者

Enokizono, Y.,Konishi, Y.,Nagata, K.,Ouhashi, K.,Uesugi, S.,Ishikawa, F.,Katahira, M. (登録日: 2005-03-22, 公開日: 2005-04-05, 最終更新日: 2024-05-29)

主引用文献

Enokizono, Y.,Konishi, Y.,Nagata, K.,Ouhashi, K.,Uesugi, S.,Ishikawa, F.,Katahira, M.
Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D.
J.Biol.Chem., 280:18862-18870, 2005

PubMed Abstract: Heterogeneous nuclear ribonucleoprotein D, also known as AUF1, has two DNA/RNA-binding domains, each of which can specifically bind to single-stranded d(TTAGGG)n, the human telomeric repeat. Here, the structure of the C-terminal-binding domain (BD2) complexed with single-stranded d(TTAGGG) determined by NMR is presented. The structure has revealed that each residue of the d(TAG) segment is recognized by BD2 in a base-specific manner. The interactions deduced from the structure have been confirmed by gel retardation experiments with mutant BD2 and DNA. It is known that single-stranded DNA with the telomeric repeat tends to form a quadruplex and that the quadruplex has an inhibitory effect on telomere elongation by telomerase. This time it is revealed that BD2 unfolds the quadruplex of such DNA upon binding. Moreover, the effect of BD2 on the elongation by telomerase was examined in vitro. These results suggest the possible involvement of heterogeneous nuclear ribonucleoprotein D in maintenance of the telomere 3'-overhang either through protection of a single-stranded DNA or destabilization of the potentially deleterious quadruplex structure for the elongation by telomerase.

PubMed: 15734733
DOI: 10.1074/jbc.M411822200

実験手法

SOLUTION NMR