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Beta-Alpha-Beta Motif

This motif comprises a beta strand-loop-helix-loop-strand arrangment, with the strands lying parallel and hydrogen-bonded to the helix. The alpha helix packs against the beta strands and thus buries the hydrophobic side chains in these strands. The joining loops regions in the motif can vary in length from one residue to more than 100 residues. 99% of these motifs are right handed.

References

Handedness of crossover connections in beta sheets.
Richardson JS
Proc Natl Acad Sci U S A73p2619-23(1976 Aug)
Logical analysis of the mechanism of protein folding. IV. Super-secondary structures.
Nagano K
J Mol Biol109p235-50(1977 Jan 15)
On the conformation of proteins: the handedness of the beta-strand-alpha-helix-beta-strand unit.
Sternberg MJ, Thornton JM
J Mol Biol105p367-82(1976 Aug 15)

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