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

Nat Struct Biol. 1997 Jul;4(7):586-91. doi: 10.1038/nsb0797-586.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray / methods
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Dimerization
  • Homeodomain Proteins*
  • Hydrogen Bonding
  • Models, Molecular
  • Protein Conformation
  • Zinc / metabolism*
  • Zinc Fingers

Substances

  • DNA-Binding Proteins
  • Homeodomain Proteins
  • RAG-1 protein
  • Zinc