Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 pentadecameric 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.
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 J Mol Biol. 2007 Mar 30;367(3):603-8. Epub 2006 Nov 3. PMID:17292396[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ James LC, Jones PC, McCoy A, Tennent GA, Pepys MB, Famm K, Winter G. Beta-edge interactions in a pentadecameric human antibody V kappa domain. J Mol Biol. 2007 Mar 30;367(3):603-8. Epub 2006 Nov 3. PMID:17292396 doi:10.1016/j.jmb.2006.10.093
