| Autor: |
Bellon SF; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA., Rodgers KK, Schatz DG, Coleman JE, Steitz TA |
| Jazyk: |
angličtina |
| Zdroj: |
Nature structural biology [Nat Struct Biol] 1997 Jul; Vol. 4 (7), pp. 586-91. |
| DOI: |
10.1038/nsb0797-586 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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