2bx5

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(New page: 200px<br /> <applet load="2bx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bx5, resolution 2.7&Aring;" /> '''IS FR1 THE ANTIBODY'...)
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Revision as of 07:41, 18 November 2007

Image:2bx5.gif

2bx5, resolution 2.7Å

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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

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