Affordable Access

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

Authors
  • Kim, MS
  • Lapkouski, M
  • Yang, W
  • Gellert, M
Publication Date
Feb 26, 2015
Source
[email protected]
Keywords
License
Unknown
External links

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. / 1 / 1 / 58 / 39 / scie / scopus

Report this publication

Statistics

Seen <100 times