1VFC

Solution Structure Of The DNA Complex Of Human Trf2

1VFC の概要

• エントリーDOI: 10.2210/pdb1vfc/pdb
• 関連するPDBエントリー: 1VF9
• 分子名称: Short G-rich strand, Short C-rich starnd, Telomeric repeat binding factor 2 (3 entities in total)
• 機能のキーワード: myb, helix-turn-helix, telomere, protein-dna complex, structural protein-dna complex, structural protein/dna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q15554
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 15363.66

構造登録者

Nishimura, Y.,Hanaoka, S. (登録日: 2004-04-12, 公開日: 2005-05-17, 最終更新日: 2023-12-27)

主引用文献

Hanaoka, S.,Nagadoi, A.,Nishimura, Y.
Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities
Protein Sci., 14:119-130, 2005

PubMed Abstract: Mammalian telomeres consist of long tandem arrays of double-stranded telomeric TTAGGG repeats packaged by the telomeric DNA-binding proteins TRF1 and TRF2. Both contain a similar C-terminal Myb domain that mediates sequence-specific binding to telomeric DNA. In a DNA complex of TRF1, only the single Myb-like domain consisting of three helices can bind specifically to double-stranded telomeric DNA. TRF2 also binds to double-stranded telomeric DNA. Although the DNA binding mode of TRF2 is likely identical to that of TRF1, TRF2 plays an important role in the t-loop formation that protects the ends of telomeres. Here, to clarify the details of the double-stranded telomeric DNA-binding modes of TRF1 and TRF2, we determined the solution structure of the DNA-binding domain of human TRF2 bound to telomeric DNA; it consists of three helices, and like TRF1, the third helix recognizes TAGGG sequence in the major groove of DNA with the N-terminal arm locating in the minor groove. However, small but significant differences are observed; in contrast to the minor groove recognition of TRF1, in which an arginine residue recognizes the TT sequence, a lysine residue of TRF2 interacts with the TT part. We examined the telomeric DNA-binding activities of both DNA-binding domains of TRF1 and TRF2 and found that TRF1 binds more strongly than TRF2. Based on the structural differences of both domains, we created several mutants of the DNA-binding domain of TRF2 with stronger binding activities compared to the wild-type TRF2.

PubMed: 15608118
DOI: 10.1110/ps.04983705

実験手法

SOLUTION NMR