期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 367, 期 3, 页码 603-608出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.10.093
关键词
beta-edge; amyloid; aggregation; antibody; light-chain deposition disease
资金
- MRC [MC_U105115240, G7900510] Funding Source: UKRI
- Medical Research Council [G7900510, MC_U105115240] Funding Source: researchfish
- Medical Research Council [G7900510, MC_U105115240] Funding Source: Medline
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据