Publication Abstract from PubMed
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.
Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster.,Bellon SF, Rodgers KK, Schatz DG, Coleman JE, Steitz TA Nat Struct Biol. 1997 Jul;4(7):586-91. PMID:9228952[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
