4WWX

Crystal structure of the core RAG1/2 recombinase

4WWX の概要

• エントリーDOI: 10.2210/pdb4wwx/pdb
• 分子名称: V(D)J recombination-activating protein 1, V(D)J recombination-activating protein 2, ZINC ION (3 entities in total)
• 機能のキーワード: v(d)j recombination, rag1/2, recombination activating gene 1/2, crystal structure., hydrolase, ligase
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Nucleus : P15919 P21784
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 219721.90

構造登録者

Kim, M.S.,Lapkouski, M.,Yang, W.,Gellert, M. (登録日: 2014-11-12, 公開日: 2015-02-25, 最終更新日: 2024-02-28)

主引用文献

Kim, M.S.,Lapkouski, M.,Yang, W.,Gellert, M.
Crystal structure of the V(D)J recombinase RAG1-RAG2.
Nature, 518:507-511, 2015

PubMed Abstract: V(D)J recombination in the vertebrate immune system generates a highly diverse population of immunoglobulins and T-cell receptors by combinatorial joining of segments of coding DNA. The RAG1-RAG2 protein complex initiates this site-specific recombination by cutting DNA at specific sites flanking the coding segments. Here we report the crystal structure of the mouse RAG1-RAG2 complex at 3.2 Å resolution. The 230-kilodalton RAG1-RAG2 heterotetramer is 'Y-shaped', with the amino-terminal domains of the two RAG1 chains forming an intertwined stalk. Each RAG1-RAG2 heterodimer composes one arm of the 'Y', with the active site in the middle and RAG2 at its tip. The RAG1-RAG2 structure rationalizes more than 60 mutations identified in immunodeficient patients, as well as a large body of genetic and biochemical data. The architectural similarity between RAG1 and the hairpin-forming transposases Hermes and Tn5 suggests the evolutionary conservation of these DNA rearrangements.

PubMed: 25707801
DOI: 10.1038/nature14174

実験手法

X-RAY DIFFRACTION (3.2001 Å)