2bx5

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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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[[Image:2bx5.jpg|left|200px]]
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caption="2bx5, resolution 2.7&Aring;" />
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'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL'''<br />
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{{Structure
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|PDB= 2bx5 |SIZE=350|CAPTION= <scene name='initialview01'>2bx5</scene>, resolution 2.7&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL'''
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==Overview==
==Overview==
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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://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX5 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17292396 17292396]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:32 2008''
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''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


PDB ID 2bx5

Drag the structure with the mouse to rotate
, resolution 2.7Å
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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