1aif

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(New page: 200px<br /> <applet load="1aif" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aif, resolution 2.9&Aring;" /> '''ANTI-IDIOTYPIC FAB 4...)
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<applet load="1aif" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1aif, resolution 2.9&Aring;" />
caption="1aif, resolution 2.9&Aring;" />
'''ANTI-IDIOTYPIC FAB 409.5.3 (IGG2A) FAB FROM MOUSE'''<br />
'''ANTI-IDIOTYPIC FAB 409.5.3 (IGG2A) FAB FROM MOUSE'''<br />
==Overview==
==Overview==
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The crystal structure of anti-idiotopic Fab 409.5.3, made against an E2, specific feline infectious peritonitis virus-neutralizing antibody, 730.1.4, has been determined in its free from, at 2.9 A resolution by, molecular replacement. This antibody, used as an immmunogen, elicits the, production of anti-anti-idiotypic antibodies that in turn neutralize the, virus. The structure of the uncomplexed Fab was refined using, constrained-restrained least squares minimization and simulated annealing, in combination with conjugate gradient techniques to a crystallographic R, of 0.22 based on 16,482 unique reflections between 20.0 and 2.9 A. The, free antiidiotypic Fab shows, when compared to its complexed form, a 5, degrees rotation of its variable light with respect to its variable heavy, domain and rearrangement of complementarity determining region loops, which permits optimization of the stereocomplementarity between, interacting molecules. This finding supports the induced fit hypothesis, for antibody antigen interaction.
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The crystal structure of anti-idiotopic Fab 409.5.3, made against an E2 specific feline infectious peritonitis virus-neutralizing antibody 730.1.4, has been determined in its free from, at 2.9 A resolution by molecular replacement. This antibody, used as an immmunogen, elicits the production of anti-anti-idiotypic antibodies that in turn neutralize the virus. The structure of the uncomplexed Fab was refined using constrained-restrained least squares minimization and simulated annealing in combination with conjugate gradient techniques to a crystallographic R of 0.22 based on 16,482 unique reflections between 20.0 and 2.9 A. The free antiidiotypic Fab shows, when compared to its complexed form, a 5 degrees rotation of its variable light with respect to its variable heavy domain and rearrangement of complementarity determining region loops, which permits optimization of the stereocomplementarity between interacting molecules. This finding supports the induced fit hypothesis for antibody antigen interaction.
==About this Structure==
==About this Structure==
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1AIF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AIF OCA].
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1AIF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIF OCA].
==Reference==
==Reference==
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[[Category: v region]]
[[Category: v region]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:26:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:48 2008''

Revision as of 09:44, 21 February 2008

Image:1aif.gif

1aif, resolution 2.9Å

Drag the structure with the mouse to rotate

ANTI-IDIOTYPIC FAB 409.5.3 (IGG2A) FAB FROM MOUSE

Overview

The crystal structure of anti-idiotopic Fab 409.5.3, made against an E2 specific feline infectious peritonitis virus-neutralizing antibody 730.1.4, has been determined in its free from, at 2.9 A resolution by molecular replacement. This antibody, used as an immmunogen, elicits the production of anti-anti-idiotypic antibodies that in turn neutralize the virus. The structure of the uncomplexed Fab was refined using constrained-restrained least squares minimization and simulated annealing in combination with conjugate gradient techniques to a crystallographic R of 0.22 based on 16,482 unique reflections between 20.0 and 2.9 A. The free antiidiotypic Fab shows, when compared to its complexed form, a 5 degrees rotation of its variable light with respect to its variable heavy domain and rearrangement of complementarity determining region loops, which permits optimization of the stereocomplementarity between interacting molecules. This finding supports the induced fit hypothesis for antibody antigen interaction.

About this Structure

1AIF is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of an anti-idiotypic Fab against feline peritonitis virus-neutralizing antibody and a comparison with the complexed Fab., Ban N, Escobar C, Hasel KW, Day J, Greenwood A, McPherson A, FASEB J. 1995 Jan;9(1):107-14. PMID:7821749

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