A Novel 11-Residue Coiled-Coil Motif Predicts a Histidine Zipper
- 1 April 1996
- journal article
- Published by Bentham Science Publishers Ltd. in Protein & Peptide Letters
- Vol. 3 (2) , 139-145
- https://doi.org/10.2174/092986650302220614124810
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.Keywords
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