Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2188288 | Journal of Molecular Biology | 2007 | 6 Pages |
Abstract
Antibodies are the archetypal molecules of the Ig-fold superfamily. Their highly conserved β-sheet architecture has evolved to avoid aggregation by protecting edge strands. However, the crystal structure of a human Vκ domain described here, reveals an exposed β-edge strand which mediates assembly of a helical pentadecameric oligomer. This edge strand is highly conserved in Vκ domains but is both shortened and capped by the use of two sequential trans-proline residues in Vλ domains. We suggest that the exposure of this β-edge in Vκ domains may explain why light-chain deposition disease is mediated predominantly by κ antibodies.
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Authors
Leo C. James, Phil C. Jones, Airlie McCoy, Glenys A. Tennent, Mark B. Pepys, Kristoffer Famm, Greg Winter,