Crystal structure of the V(D)J recombinase RAG1-RAG2
SCIE
SCOPUS
- Title
- Crystal structure of the V(D)J recombinase RAG1-RAG2
- Authors
- Kim, MS; Lapkouski, M; Yang, W; Gellert, M
- Date Issued
- 2015-02-26
- Publisher
- Nature Publishing Group
- 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 3.2A 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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/39385
- DOI
- 10.1038/nature14174
- ISSN
- 0028-0836
- Article Type
- Article
- Citation
- NATURE, vol. 518, no. 7540, page. 507 - 511, 2015-02-26
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- There are no files associated with this item.
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