Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis-Reference-Cited by-同舟云学术

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Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis

Published:2009-04-26 Issue:5 Volume:16 Page:499-508
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Yin Fang Fang,Bailey Scott,Innis C Axel,Ciubotaru Mihai,Kamtekar Satwik,Steitz Thomas A,Schatz David G

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.1593.pdf

Reference60 articles.

1. Schatz, D.G., Oettinger, M.A. & Baltimore, D. The V(D)J recombination activating gene, RAG-1. Cell 59, 1035–1048 (1989).

2. Oettinger, M.A., Schatz, D.G., Gorka, C. & Baltimore, D. RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination. Science 248, 1517–1523 (1990).

3. Sawchuk, D.J. et al. V(D)J recombination: modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins. J. Exp. Med. 185, 2025–2032 (1997).

4. van Gent, D.C., Hiom, K., Paull, T.T. & Gellert, M. Stimulation of V(D)J cleavage by high mobility group proteins. EMBO J. 16, 2665–2670 (1997).

5. Tonegawa, S. Somatic generation of antibody diversity. Nature 302, 575–581 (1983).

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