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

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)