2bx5

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bx5 OCA], [http://www.ebi.ac.uk/pdbsum/2bx5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bx5 RCSB]</span>
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[[Category: light-chain]]
[[Category: light-chain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:07:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:13:07 2008''

Revision as of 23:13, 30 March 2008

Image:2bx5.jpg


PDB ID 2bx5

Drag the structure with the mouse to rotate
, resolution 2.7Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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