1Z1D

Structural Model for the interaction between RPA32 C-terminal domain and SV40 T antigen origin binding domain.

1Z1D の概要

• エントリーDOI: 10.2210/pdb1z1d/pdb
• 関連するPDBエントリー: 1DPU 1TBD
• 分子名称: Replication protein A 32 kDa subunit, Large T antigen (2 entities in total)
• 機能のキーワード: winged helix-turn-helix motif, origin binding domain, protein-protein complex, replication
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P15927; Host nucleus: P03070
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26110.49

構造登録者

Arunkumar, A.I.,Klimovich, V.,Jiang, X.,Ott, R.D.,Mizoue, L.,Fanning, E.,Chazin, W.J. (登録日: 2005-03-03, 公開日: 2005-05-17, 最終更新日: 2024-05-22)

主引用文献

Arunkumar, A.I.,Klimovich, V.,Jiang, X.,Ott, R.D.,Mizoue, L.,Fanning, E.,Chazin, W.J.
Insights into hRPA32 C-terminal domain--mediated assembly of the simian virus 40 replisome.
Nat.Struct.Mol.Biol., 12:332-339, 2005

PubMed Abstract: Simian virus 40 (SV40) provides a model system for the study of eukaryotic DNA replication, in which the viral protein, large T antigen (Tag), marshals human proteins to replicate the viral minichromosome. SV40 replication requires interaction of Tag with the host single-stranded DNA-binding protein, replication protein A (hRPA). The C-terminal domain of the hRPA32 subunit (RPA32C) facilitates initiation of replication, but whether it interacts with Tag is not known. Affinity chromatography and NMR revealed physical interaction between hRPA32C and the Tag origin DNA-binding domain, and a structural model of the complex was determined. Point mutations were then designed to reverse charges in the binding sites, resulting in substantially reduced binding affinity. Corresponding mutations introduced into intact hRPA impaired initiation of replication and primosome activity, implying that this interaction has a critical role in assembly and progression of the SV40 replisome.

PubMed: 15793585
DOI: 10.1038/nsmb916

実験手法

SOLUTION NMR