1eo8

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(New page: 200px<br /> <applet load="1eo8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eo8, resolution 2.8&Aring;" /> '''INFLUENZA VIRUS HEMA...)
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[[Image:1eo8.gif|left|200px]]<br />
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[[Image:1eo8.gif|left|200px]]<br /><applet load="1eo8" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1eo8" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1eo8, resolution 2.8&Aring;" />
caption="1eo8, resolution 2.8&Aring;" />
'''INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY'''<br />
'''INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY'''<br />
==Overview==
==Overview==
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The structure of a complex between the hemagglutinin of influenza virus, and the Fab of a neutralizing antibody was determined by X-ray, crystallography at 2.8 A resolution. This antibody and another which has, only 56% sequence identity bind to the same epitope with very similar, affinities and in the same orientation. One third of the interactions is, conserved in the two complexes; a significant proportion of the, interactions that differ are established by residues of the H3, complementarity-determining regions (CDR) which adopt distinct, conformations in the two antibodies. This demonstrates that there is a, definite flexibility in the selection of antibodies that bind to a given, epitope, despite the high affinity of their complexes. This flexibility, allows the humoral immune response to be redundant, a feature that may be, useful in achieving longer lasting protection against evolving viral, pathogens.
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The structure of a complex between the hemagglutinin of influenza virus and the Fab of a neutralizing antibody was determined by X-ray crystallography at 2.8 A resolution. This antibody and another which has only 56% sequence identity bind to the same epitope with very similar affinities and in the same orientation. One third of the interactions is conserved in the two complexes; a significant proportion of the interactions that differ are established by residues of the H3 complementarity-determining regions (CDR) which adopt distinct conformations in the two antibodies. This demonstrates that there is a definite flexibility in the selection of antibodies that bind to a given epitope, despite the high affinity of their complexes. This flexibility allows the humoral immune response to be redundant, a feature that may be useful in achieving longer lasting protection against evolving viral pathogens.
==About this Structure==
==About this Structure==
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1EO8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EO8 OCA].
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1EO8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EO8 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Bizebard, T.]]
[[Category: Bizebard, T.]]
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[[Category: Daniels, R.S.]]
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[[Category: Daniels, R S.]]
[[Category: Fleury, D.]]
[[Category: Fleury, D.]]
[[Category: Gigant, B.]]
[[Category: Gigant, B.]]
[[Category: Knossow, M.]]
[[Category: Knossow, M.]]
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[[Category: Skehel, J.J.]]
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[[Category: Skehel, J J.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: complex (hemagglutinin/immmunoglobulin)]]
[[Category: complex (hemagglutinin/immmunoglobulin)]]
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[[Category: viral protein]]
[[Category: viral protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:29:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:49 2008''

Revision as of 10:29, 21 February 2008


1eo8, resolution 2.8Å

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INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY

Overview

The structure of a complex between the hemagglutinin of influenza virus and the Fab of a neutralizing antibody was determined by X-ray crystallography at 2.8 A resolution. This antibody and another which has only 56% sequence identity bind to the same epitope with very similar affinities and in the same orientation. One third of the interactions is conserved in the two complexes; a significant proportion of the interactions that differ are established by residues of the H3 complementarity-determining regions (CDR) which adopt distinct conformations in the two antibodies. This demonstrates that there is a definite flexibility in the selection of antibodies that bind to a given epitope, despite the high affinity of their complexes. This flexibility allows the humoral immune response to be redundant, a feature that may be useful in achieving longer lasting protection against evolving viral pathogens.

About this Structure

1EO8 is a Protein complex structure of sequences from Influenza a virus and Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural evidence for recognition of a single epitope by two distinct antibodies., Fleury D, Daniels RS, Skehel JJ, Knossow M, Bizebard T, Proteins. 2000 Sep 1;40(4):572-8. PMID:10899782

Page seeded by OCA on Thu Feb 21 12:29:49 2008

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