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A low-resolution structure of the bacterial toxin colicin la provides a model for its lethal membrane association and an explanation for the anomalous behaviour of its C-terminal peptide fragment.
The X-ray crystal structure of endothelin reveals a peptide with a compact globular conformation that may well represent the active form of the molecule.
Variation in ways in which proteins can identify and lock on to genes due for transcription is illuminated by studies of the Arc represser, which has a β-sheet, rather than α-helical, recognition motif.
The biological relevance of the i-motif comes under examination with the structural characterization of oligonucleotides formed of repeats of the human telomeric C-strand sequence d(CCCTAA)n.
The first issue of this new monthly journal provides a variety of papers for structural biologists (and others) to get their teeth into, among them two dealing with the intriguing matter of protein folding.
