2BX5

Is FR1 the antibody's Achillies heel

Summary for 2BX5

Entry DOI	10.2210/pdb2bx5/pdb
Descriptor	VD9 VKI LIGHT-CHAIN (2 entities in total)
Functional Keywords	immune system, amyloid, lcdd, antibody, aggregation, fr1
Biological source	HOMO SAPIENS (HUMAN)
Total number of polymer chains	15
Total formula weight	173110.99
Authors	James, L.C. (deposition date: 2005-07-22, release date: 2006-11-15, Last modification date: 2024-10-23)
Primary citation	James, L.C.,Jones, P.C.,Mccoy, A.,Tennent, G.A.,Pepys, M.B.,Famm, K.,Winter, G. Beta-Edge Interactions in a Pentadecameric Human Antibody Vkappa Domain. J.Mol.Biol., 367:603-, 2007 Cited by PubMed 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 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. PubMed: 17292396 DOI: 10.1016/J.JMB.2006.10.093 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation