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PROSITE documentation PDOC51765

Zinc finger RAG1-type profile





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

ZF_RAG1, PS51765; Zinc finger RAG1-type profile  (MATRIX)


References

1AuthorsBellon S.F. Rodgers K.K. Schatz D.G. Coleman J.E. Steitz T.A.
TitleCrystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster.
SourceNat. Struct. Biol. 4:586-591(1997).
PubMed ID9228952

2AuthorsJones J.M. Gellert M.
TitleAutoubiquitylation of the V(D)J recombinase protein RAG1.
SourceProc. Natl. Acad. Sci. U.S.A. 100:15446-15451(2003).
PubMed ID14671314
DOI10.1073/pnas.2637012100

3AuthorsMao M.-G. Lei J.-L. Alex P.-M. Hong W.-S. Wang K.-J.
TitleCharacterization of RAG1 and IgM (mu chain) marking development of the immune system in red-spotted grouper (Epinephelus akaara).
SourceFish Shellfish Immunol. 33:725-735(2012).
PubMed ID22796426
DOI10.1016/j.fsi.2012.06.011



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