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• W2012238315 endingPage "511" @default.
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• W2012238315 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. The crystal structure of the RAG1–RAG2 heterotetramer forms a Y-shaped structure, with each arm containing a RAG1–RAG2 heterodimer; the overall structure is reminiscent of hairpin-forming transposases, attesting to its evolutionary history as a specialized form of a transposition activity. The vertebrate immune system uses V(D)J recombination to generate a vast array of different genes encoding immunoglobulins and T-cell receptors from a limited repertoire of coding segments. The recombination process is initiated by the cleavage complex, RAG1–RAG2. Wei Yang and colleagues have now solved the crystal structure of the RAG1–RAG2 recombinase heterotetramer at 3.2 Å resolution. The complex forms a Y-shaped structure, with each arm containing a RAG1–RAG2 heterodimer. The overall structure resembles that of hairpin-forming transposases, attesting to its evolutionary history as a specialized form of a transposition activity. The structure provides insight into the mechanism of V(D)J recombination and the basis for many disease-causing mutations." @default.
• W2012238315 created "2016-06-24" @default.
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• W2012238315 creator A5017411047 @default.
• W2012238315 creator A5067566788 @default.
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• W2012238315 date "2015-02-18" @default.
• W2012238315 modified "2023-09-30" @default.
• W2012238315 title "Crystal structure of the V(D)J recombinase RAG1–RAG2" @default.
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• W2012238315 doi "https://doi.org/10.1038/nature14174" @default.
• W2012238315 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4342785" @default.
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• W2012238315 hasPublicationYear "2015" @default.
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