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. 1981 Jul;78(7):4146–4150. doi: 10.1073/pnas.78.7.4146

Relative orientation of close-packed β-pleated sheets in proteins

Cyrus Chothia *,†, Joël Janin ‡
PMCID: PMC319745  PMID: 16593054

Abstract

When β-pleated sheets pack face to face in proteins, the angle between the strand directions of the two β-sheets is observed to be near -30°. We propose a simple model for β-sheet-to-β-sheet packing in concanavalin A, plastocyanin, γ-crystallin, superoxide dismutase, prealbumin, and the immunoglobin fragment VREI. This model shows how the observed relative orientation of two packed β-sheets is a consequence of (i) the rows of side chains at the interface being approximately aligned and (ii) the β-sheet having a right-handed twist. The special amino acid composition of residues at the β-sheet-to-β-sheet interfaces makes the contact surfaces essentially smooth and hydrophobic.

Keywords: twisted β-sheets, protein secondary and tertiary structure

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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