5FOX

HUMANISED MONOMERIC RADA IN COMPLEX WITH FHAA TETRAPEPTIDE

5FOX の概要

• エントリーDOI: 10.2210/pdb5fox/pdb
• 関連するPDBエントリー: 5FOS 5FOT 5FOU 5FOV 5FOW
• 分子名称: DNA REPAIR AND RECOMBINATION PROTEIN RADA, FHAA PEPTIDE, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, rada, fxxa motif, recombinase
• 由来する生物種: PYROCOCCUS FURIOSUS; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26158.75

構造登録者

Scott, D.E.,Marsh, M.,Blundell, T.L.,Abell, C.,Hyvonen, M. (登録日: 2015-11-26, 公開日: 2016-03-30, 最終更新日: 2024-10-16)

主引用文献

Scott, D.E.,Marsh, M.,Blundell, T.L.,Abell, C.,Hyvonen, M.
Structure Activity Relationship of the Peptide Binding Motif Mediating the Rad51:Brca2 Protein-Protein Interaction.
FEBS Lett., 590:1094-, 2016

PubMed Abstract: RAD51 is a recombinase involved in the homologous recombination of double-strand breaks in DNA. RAD51 forms oligomers by binding to another molecule of RAD51 via an 'FxxA' motif, and the same recognition sequence is similarly utilised to bind BRCA2. We have tabulated the effects of mutation of this sequence, across a variety of experimental methods and from relevant mutations observed in the clinic. We use mutants of a tetrapeptide sequence to probe the binding interaction, using both isothermal titration calorimetry and X-ray crystallography. Where possible, comparison between our tetrapeptide mutational study and the previously reported mutations is made, discrepancies are discussed and the importance of secondary structure in interpreting alanine scanning and mutational data of this nature is considered.

PubMed: 26992456
DOI: 10.1002/1873-3468.12139

実験手法

X-RAY DIFFRACTION (1.3 Å)