1RMD

RAG1 DIMERIZATION DOMAIN

Summary for 1RMD

• Entry DOI: 10.2210/pdb1rmd/pdb
• Descriptor: RAG1, ZINC ION (3 entities in total)
• Functional Keywords: rag1, v(d)j recombination, antibody, mad, ring finger, zinc binuclear cluster, zinc finger, dna-binding protein, dna binding protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus: P15919
• Total number of polymer chains: 1
• Total formula weight: 13413.09

Authors

Bellon, S.F.,Rodgers, K.K.,Schatz, D.G.,Coleman, J.E.,Steitz, T.A. (deposition date: 1997-01-10, release date: 1997-07-23, Last modification date: 2024-02-14)

Primary citation

Bellon, S.F.,Rodgers, K.K.,Schatz, D.G.,Coleman, J.E.,Steitz, T.A.
Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster.
Nat.Struct.Biol., 4:586-591, 1997

PubMed 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.

PubMed: 9228952
DOI: 10.1038/nsb0797-586

Experimental method

X-RAY DIFFRACTION (2.1 Å)