| First Author | Kim MS | Year | 2015 |
| Journal | Nature | Volume | 518 |
| Issue | 7540 | Pages | 507-11 |
| PubMed ID | 25707801 | Mgi Jnum | J:245396 |
| Mgi Id | MGI:5919821 | Doi | 10.1038/nature14174 |
| Citation | Kim MS, et al. (2015) Crystal structure of the V(D)J recombinase RAG1-RAG2. Nature 518(7540):507-11 |
| abstractText | 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 A 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. |
