4WWX
Crystal structure of the core RAG1/2 recombinase
Summary for 4WWX
| Entry DOI | 10.2210/pdb4wwx/pdb |
| Descriptor | V(D)J recombination-activating protein 1, V(D)J recombination-activating protein 2, ZINC ION (3 entities in total) |
| Functional Keywords | v(d)j recombination, rag1/2, recombination activating gene 1/2, crystal structure., hydrolase, ligase |
| Biological source | Mus musculus (Mouse) More |
| Cellular location | Nucleus : P15919 P21784 |
| Total number of polymer chains | 4 |
| Total formula weight | 219721.90 |
| Authors | Kim, M.S.,Lapkouski, M.,Yang, W.,Gellert, M. (deposition date: 2014-11-12, release date: 2015-02-25, Last modification date: 2024-02-28) |
| Primary citation | Kim, M.S.,Lapkouski, M.,Yang, W.,Gellert, M. Crystal structure of the V(D)J recombinase RAG1-RAG2. Nature, 518:507-511, 2015 Cited by 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: 25707801DOI: 10.1038/nature14174 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2001 Å) |
Structure validation
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