2bx5: Difference between revisions
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[[Image:2bx5.jpg|left|200px]] | [[Image:2bx5.jpg|left|200px]] | ||
'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL''' | {{Structure | ||
|PDB= 2bx5 |SIZE=350|CAPTION= <scene name='initialview01'>2bx5</scene>, resolution 2.7Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BX5 is a [ | 2BX5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX5 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17292396 17292396] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: light-chain]] | [[Category: light-chain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:07:56 2008'' | ||
Revision as of 14:07, 20 March 2008
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| 2bx5, resolution 2.7Å | |||||||||||||
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| 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
Page seeded by OCA on Thu Mar 20 16:07:56 2008
