2KZ3

Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83

2KZ3 の概要

• エントリーDOI: 10.2210/pdb2kz3/pdb
• NMR情報: BMRB: 16996
• 分子名称: Putative uncharacterized protein RAD51L3 (1 entity in total)
• 機能のキーワード: rad51d, homologous recombination, unknown function
• 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: 9070.67

構造登録者

Choi, N.,Kim, Y. (登録日: 2010-06-11, 公開日: 2011-01-05, 最終更新日: 2024-05-15)

主引用文献

Kim, Y.M.,Choi, B.S.
Structural and functional characterization of the N-terminal domain of human Rad51D
Int.J.Biochem.Cell Biol., 43:416-422, 2011

PubMed Abstract: Rad51D, one of five Rad51 paralogs, is required for homologous recombination and disruption of Holliday junctions with bloom syndrome protein (BLM) in vertebrates. The N-terminal domain of Rad51D is highly conserved in eukaryotic Rad51D orthologs and is essential for protein-protein interaction with XRCC2, but nothing is known about its individual structure or function. In this study, we determined the solution structure of the human Rad51D N-terminal domain (residues 1-83), which consists of four short helices flanked by long N- and C-terminal tails. Interestingly, the position of the N-terminal tail (residues 1-13) is fixed within the domain structure via several hydrophobic interactions between Leu4 and Thr27, Leu4 and Val28, and Val6 and Ile17. We show that the domain preferentially binds to ssDNA versus dsDNA and does not bind to a mobile Holliday junction by electrophoretic mobility shift assay. NMR titration and dynamics studies showed that human Rad51D-N interacts with ssDNA by positively charged and hydrophobic residues on its surface. The results suggest that the N-terminal domain of Rad51D is required for the ssDNA-specific binding function of human Rad51D and that the conserved N-terminal domains of other Rad51 paralogs may have distinguishable functions from each other in homologous recombination.

PubMed: 21111057
DOI: 10.1016/j.biocel.2010.11.014

実験手法

SOLUTION NMR