1W0U

hTRF2 DNA-binding domain in complex with telomeric DNA.

1W0U の概要

• エントリーDOI: 10.2210/pdb1w0u/pdb
• 関連するPDBエントリー: 1H6P
• 分子名称: TELOMERIC REPEAT BINDING FACTOR 2, 5'-D(*TP*CP*TP*AP*GP*GP*GP*TP*TP*AP *GP*GP*GP*TP*TP*AP*G)-3', 5'-D(*CP*TP*AP*AP*CP*CP*CP*TP*AP*AP *CP*CP*CP*TP*AP*GP*A)-3', ... (4 entities in total)
• 機能のキーワード: telomere, dna-binding protein, homeodomain, mitosis, cell cycle, nuclear protein, chromosomal protein, phosphorylation, adp-ribosylation, dna binding protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus: Q15554
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 23531.01

構造登録者

Court, R.I.,Chapman, L.M.,Fairall, L.,Rhodes, D. (登録日: 2004-06-11, 公開日: 2004-12-22, 最終更新日: 2024-05-08)

主引用文献

Court, R.I.,Chapman, L.M.,Fairall, L.,Rhodes, D.
How the Human Telomeric Proteins Trf1 and Trf2 Recognize Telomeric DNA: A View from High-Resolution Crystal Structures
Embo Rep., 6:39-, 2005

PubMed Abstract: Human telomeres consist of tandem arrays of TTAGGG sequence repeats that are specifically bound by two proteins, TRF1 and TRF2. They bind to DNA as preformed homodimers and have the same architecture in which the DNA-binding domains (Dbds) form independent structural units. Despite these similarities, TRF1 and TRF2 have different functions at telomeres. The X-ray crystal structures of both TRF1- and TRF2-Dbds in complex with telomeric DNA (2.0 and 1.8 angstroms resolution, respectively) show that they recognize the same TAGGGTT binding site by means of homeodomains, as does the yeast telomeric protein Rap1p. Two of the three G-C base pairs that characterize telomeric repeats are recognized specifically and an unusually large number of water molecules mediate protein-DNA interactions. The binding of the TRF2-Dbd to the DNA double helix shows no distortions that would account for the promotion of t-loops in which TRF2 has been implicated.

PubMed: 15608617
DOI: 10.1038/SJ.EMBOR.7400314

実験手法

X-RAY DIFFRACTION (1.8 Å)