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

Nature Structural Biology volume 4, pages 586–591 (1997) Cite this article

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 form 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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Author notes

  1. Steven F. Bellon and Karla K. Rodgers: These authors contributed equally to this work.

Authors and Affiliations

  1. Department of Molecular Biophysics and Biochemistry,

    Steven F. Bellon, Karla K. Rodgers, Joseph E. Coleman & Thomas A. Steitz

  2. Howard Hughes Medical Institute, Yale University, New Haven, Connecticut, 06520-8114, USA

    Thomas A. Steitz

  3. Howard Hughes Medical Institute, Section of Immunobiology, Yale University School of Medicine, New Haven, Connecticut, 06520-8011, USA

    David G. Schatz

Authors
  1. Steven F. Bellon
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  2. Karla K. Rodgers
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  3. David G. Schatz
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  4. Joseph E. Coleman
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  5. Thomas A. Steitz
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Bellon, S., Rodgers, K., Schatz, D. et al. Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat Struct Mol Biol 4, 586–591 (1997). https://doi.org/10.1038/nsb0797-586

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