1eo8: Difference between revisions

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[[Image:1eo8.~~gif~~|left|200px]]

[[Image:1eo8.png|left|200px]]

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~~'''~~INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY~~'''~~

===INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_10899782}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10899782 is the PubMed ID number.

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==About this Structure==

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[[Category: Immunoglobulin]]

[[Category: Viral protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:20:14 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:16:07 2008''

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-[[Image:1eo8.gif|left|200px]]
+{{Seed}}
+[[Image:1eo8.png|left|200px]]
 <!--
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 {{STRUCTURE_1eo8|  PDB=1eo8  |  SCENE=  }}
-'''INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10899782}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10899782 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10899782}}
 ==About this Structure==
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 [[Category: Immunoglobulin]]
 [[Category: Viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:20:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:16:07 2008''