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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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[[Image:2bx5.gif|left|200px]]<br />
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[[Image:2bx5.jpg|left|200px]]<br /><applet load="2bx5" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2bx5" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2bx5, resolution 2.7&Aring;" />
caption="2bx5, resolution 2.7&Aring;" />
'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL'''<br />
'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL'''<br />
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==About this Structure==
==About this Structure==
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2BX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BX5 OCA].
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2BX5 is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: light-chain]]
[[Category: light-chain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:48:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:17:34 2008''

Revision as of 15:17, 15 February 2008

Image:2bx5.jpg

2bx5, resolution 2.7Å

Drag the structure with the mouse to rotate

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 Fri Feb 15 17:17:34 2008

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