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Crystal structure of the V(D)J recombinase RAG1–RAG2

Author

Listed:
  • Min-Sung Kim

    (Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, Maryland 20892, USA)

  • Mikalai Lapkouski

    (Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, Maryland 20892, USA
    Present address: Department of Cell and Molecular Biology, Karolinska Institute, 171 77 Stockholm, Sweden, and Centre for Structural Systems Biology, DESY, 22607 Hamburg, Germany.)

  • Wei Yang

    (Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, Maryland 20892, USA)

  • Martin Gellert

    (Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, Maryland 20892, USA)

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.

Suggested Citation

  • Min-Sung Kim & Mikalai Lapkouski & Wei Yang & Martin Gellert, 2015. "Crystal structure of the V(D)J recombinase RAG1–RAG2," Nature, Nature, vol. 518(7540), pages 507-511, February.
    • Handle: RePEc:nat:nature:v:518:y:2015:i:7540:d:10.1038_nature14174
    DOI: 10.1038/nature14174
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