2bx5: Difference between revisions
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{{STRUCTURE_2bx5| PDB=2bx5 | SCENE= }} | |||
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'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL''' | '''IS FR1 THE ANTIBODY'S ACHILLIES HEEL''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: James, L C.]] | [[Category: James, L C.]] | ||
[[Category: | [[Category: Aggregation]] | ||
[[Category: | [[Category: Amyloid]] | ||
[[Category: | [[Category: Antibody]] | ||
[[Category: | [[Category: Fr1]] | ||
[[Category: | [[Category: Lcdd]] | ||
[[Category: | [[Category: Light-chain]] | ||
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Revision as of 17:55, 3 May 2008
IS FR1 THE ANTIBODY'S ACHILLIES HEEL
Overview
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.
About this Structure
2BX5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 20:55:19 2008
