1rmd

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Image:1rmd.gif

1rmd, resolution 2.10Å

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RAG1 DIMERIZATION DOMAIN

Overview

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.

About this Structure

1RMD is a Single protein structure of sequence from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.

Reference

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

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