1qfu
From Proteopedia
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|PDB= 1qfu |SIZE=350|CAPTION= <scene name='initialview01'>1qfu</scene>, resolution 2.8Å | |PDB= 1qfu |SIZE=350|CAPTION= <scene name='initialview01'>1qfu</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfu OCA], [http://www.ebi.ac.uk/pdbsum/1qfu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qfu RCSB]</span> | ||
}} | }} | ||
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[[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]] | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''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 23:12:55 2008'' |
Revision as of 20:12, 30 March 2008
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| , 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 of influenza hemagglutinin (HA) with a neutralizing antibody shows that the antibody binds to HA at a distance from the virus receptor binding site. Comparison of the properties of this antibody and its Fab with those of an antibody that recognizes an epitope overlapping the receptor binding site leads to two main conclusions. First, inhibition of receptor binding is an important component of neutralization. Second, the efficiency of neutralization by the antibodies ranks in the same order as their avidities for HA, and their large size makes these antibodies highly efficient at neutralization, regardless of the location of their epitope in relation to the virus receptor binding site. These observations provide rationales for the range of antibody specificities that are detected in immune sera and for the distribution of sequence changes on the membrane-distal surface of influenza HAs that occur during 'antigenic drift.'
About this Structure
1QFU is a Single protein structure of sequence from Influenza a virus and Mus musculus. The following page contains interesting information on the relation of 1QFU with [Hemagglutinin]. Full crystallographic information is available from OCA.
Reference
A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site., Fleury D, Barrere B, Bizebard T, Daniels RS, Skehel JJ, Knossow M, Nat Struct Biol. 1999 Jun;6(6):530-4. PMID:10360354
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