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1eo8
From Proteopedia
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|PDB= 1eo8 |SIZE=350|CAPTION= <scene name='initialview01'>1eo8</scene>, resolution 2.8Å | |PDB= 1eo8 |SIZE=350|CAPTION= <scene name='initialview01'>1eo8</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eo8 OCA], [http://www.ebi.ac.uk/pdbsum/1eo8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eo8 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Knossow, M.]] | [[Category: Knossow, M.]] | ||
[[Category: Skehel, J J.]] | [[Category: Skehel, J J.]] | ||
| - | [[Category: NAG]] | ||
[[Category: complex (hemagglutinin/immmunoglobulin)]] | [[Category: complex (hemagglutinin/immmunoglobulin)]] | ||
[[Category: hemagglutinin]] | [[Category: hemagglutinin]] | ||
| Line 36: | Line 38: | ||
[[Category: viral protein]] | [[Category: viral protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:06:28 2008'' |
Revision as of 17:06, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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