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Volume 10 Issue 7, July 2003

The crystal structure of a soluble mouse furin fragment (purple surface and ribbon) in complex with a peptide inhibitor (green and red model). Furin cleaves a wide range of proproteins, such as growth factors, and activates several bacterial toxins, including the anthrax toxin. The structure provides insights into the substrate specificity of furin. See pages 520-526.

Volume 10 Issue 7

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  • The structure of the dimeric replication initiator of pPS10 reveals that secondary structure remodeling of chameleon sequences defines the monomer-dimer oligomerization state of the protein. Together with an unanticipated dimerization interface, this result will steer thinking in the field and influence strategies to control spread of virulence and antibiotic resistance genes that are often plasmid-encoded.

    • Katrina T Forest
    • Marcin S Filutowicz
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  • Two recent papers provide evidence that the Escherichia coli RecBCD complex, which unwinds double-stranded DNA to supply a substrate for recombination, has two helicase subunits that bind opposite DNA strands and move with opposite unwinding 'polarities'.

    • Steven W Matson
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  • The structure of the CH1 domain of p300 in complex with the transactivation domain of CITED2 brings us one step closer toward understanding the molecular basis of the regulation of hypoxia response.

    • Shoumo Bhattacharya
    • Peter J Ratcliffe
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