| Literature DB >> 9228952 |
S F Bellon1, K K Rodgers, D G Schatz, J E Coleman, T A Steitz.
Abstract
The crystal structure of the dimerization domain of the V(D)J recombination-activating protein, RAG1, was solved using zinc anomalous scattering. The structure reveals an unusual combination of multi-class zinc-binding motifs, including a zinc RING finger and a C2H2 zinc finger, that together from a single structural domain. The domain also contains a unique zinc binuclear cluster in place of a normally mononuclear zinc site in the RING finger. Together, four zinc ions help organize the entire domain, including the two helices that form the dimer interface.Entities:
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Year: 1997 PMID: 9228952 DOI: 10.1038/nsb0797-586
Source DB: PubMed Journal: Nat Struct Biol ISSN: 1072-8368