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beta-edge interactions in a pentadecameric human antibody V kappa domain

James, LC; Jones, PC; Mccoy, A; Tennent, GA; Pepys, MB; Famm, K; Winter, G; (2007) beta-edge interactions in a pentadecameric human antibody V kappa domain. J MOL BIOL , 367 (3) 603 - 608. 10.1016/j.jmb.2006.10.093.

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Abstract

Antibodies are the archetypal molecules of the Ig-fold superfamily. Their highly conserved beta-sheet architecture has evolved to avoid aggregation by protecting edge strands. However, the crystal structure of a human V kappa domain described here, reveals an exposed beta-edge strand which mediates assembly of a helical pentaclecameric oligomer. This edge strand is highly conserved in V kappa domains but is both shortened and capped by the use of two sequential trans-proline residues in V lambda domains. We suggest that the exposure of this beta-edge in V kappa domains may explain why light-chain deposition disease is mediated predominantly by kappa antibodies. (c) 2007 Published by Elsevier Ltd.

Type: Article
Title: beta-edge interactions in a pentadecameric human antibody V kappa domain
DOI: 10.1016/j.jmb.2006.10.093
Keywords: beta-edge, amyloid, aggregation, antibody, light-chain deposition disease, CHAIN-DEPOSITION-DISEASE, LIGHT-CHAIN, AGGREGATION, PROTEINS, REVEALS
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine > Inflammation
URI: http://discovery.ucl.ac.uk/id/eprint/90706
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