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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The amino terminal regions of proBNP and proANP oligomerise through leucine zipper-like coiled-coil motifs.

We provide the first report of unique leucine zipper-like coiled-coil sequence motifs at the amino terminus (N-) of proBrain Natriuretic Peptide (proBNP) and proAtrial Natriuretic Peptide (proANP). These motifs were highly conserved across most of the known natriuretic peptide sequences from different species. Consistent with computer based modelling predictions, size exclusion (SE) chromatography analysis confirmed human and ovine N-BNP, N-ANP and human proBNP in plasma extracts to elute as high molecular weight oligomers. Synthetic model peptides corresponding to the proposed leucine zipper-like coiled-coil regions of proBNP, proANP and their related N-terminal peptides were shown to be sufficient to induce oligomerisation when assessed on size exclusion HPLC. To our knowledge, this is the first report of circulating peptides that oligomerise through leucine zipper-like coiled-coil motifs, and adds a new dimension to the field of vasoactive peptide research.[1]

References

  1. The amino terminal regions of proBNP and proANP oligomerise through leucine zipper-like coiled-coil motifs. Seidler, T., Pemberton, C., Yandle, T., Espiner, E., Nicholls, G., Richards, M. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
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