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Publication : Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster.

First Author  Bellon SF Year  1997
Journal  Nat Struct Biol Volume  4
Issue  7 Pages  586-91
PubMed ID  9228952 Mgi Jnum  J:159276
Mgi Id  MGI:4442154 Doi  10.1038/nsb0797-586
Citation  Bellon SF, et al. (1997) Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat Struct Biol 4(7):586-91
abstractText  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.
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