Structural models of the evolutionarily conservative central domain of silk-moth chorion proteins

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Abstract
Silk-moth chorion proteins belong to a small number of families: A, B, C, Hc-A and Hc-B. The central domain is an evolutionarily conservative region in each family, of variable length and composition between families. This domain shows dear 6-fold periodicities for various amino acid residues, e.g. glycine. The periodicities, together with the well-documented prevalence of β-sheet and β-turn secondary structure of chorion proteins, strongly support a structural model in which four-residue β-strands alternate with β-turns, forming a compact antiparallel, probably twisted β-sheet. Conformational analysis, aided by interactive graphics refinement and recent experimental findings, further suggest that this structure consists of β-strands, alternating with I′ and II′ β-turns, and apparently forms the basis for the molecular and supramolecular assembly of chorion.

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