A Novel 11-Residue Coiled-Coil Motif Predicts a Histidine Zipper

Abstract
A protein sequence is described that consists of a highly repeated 11-mer motif. The motif has the characteristics of an α -helical coilled-coil but contains, in addition, a highly conserved histidine position that lies centrally on the hydrophobic face of the amphipathic helix. The sequence was modelled as ei­ ther a three or four stranded coilled-coil with the histidines hydrogen-bonded . (like a zipper) in the core.

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