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PROSITE documentation PDOC51765Zinc finger RAG1-type profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51765
The development of B and T cells depends on the rearrangement of variable (V), diversity (D), and joining (J) gene segments to produce mature Ig and T cell receptor coding regions. This rearrangement process, known as V(D)J recombination is initiated by the complex, multi-domain proteins RAG1 and RAG2. The RAG proteins catalyze DNA cleavage in the first phase of the reaction using a recombination signal sequence (RSS) that flanks V, D and J segments [1,2,3].
RAG1 contains a zinc-binding dimerization domain immediately N-terminal to the catalytic core region, which in turn contains a putative DNA-binding domain (see <PDOC51487>) at its N terminus. The dimerization domain consists of a zinc C3HC4 RING finger (see <PDOC00449>) and a C2H2 zinc RAG1-type finger.
The C2H2 RAG1-type zinc finger contains the hallmarks of a classical zinc finger structure with a two stranded β-sheet and an α-helix (see <PDB:1RMD>) [1].
The profile we developed covers the entire RAG1-type zinc finger.
Last update:July 2015 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Bellon S.F. Rodgers K.K. Schatz D.G. Coleman J.E. Steitz T.A. |
| Title | Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. | |
| Source | Nat. Struct. Biol. 4:586-591(1997). | |
| PubMed ID | 9228952 |
| 2 | Authors | Jones J.M. Gellert M. |
| Title | Autoubiquitylation of the V(D)J recombinase protein RAG1. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 100:15446-15451(2003). | |
| PubMed ID | 14671314 | |
| DOI | 10.1073/pnas.2637012100 |
| 3 | Authors | Mao M.-G. Lei J.-L. Alex P.-M. Hong W.-S. Wang K.-J. |
| Title | Characterization of RAG1 and IgM (mu chain) marking development of the immune system in red-spotted grouper (Epinephelus akaara). | |
| Source | Fish Shellfish Immunol. 33:725-735(2012). | |
| PubMed ID | 22796426 | |
| DOI | 10.1016/j.fsi.2012.06.011 |
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