1jv5
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jv5 OCA], [http://www.ebi.ac.uk/pdbsum/1jv5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jv5 RCSB]</span> | ||
}} | }} | ||
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[[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 21:39:29 2008'' |
Revision as of 18:39, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Anti-blood group A Fv
Overview
The specificity of antibody recognition of the ABO blood group trisaccharide antigens has been explored by crystal structure analysis and mutation methods. The crystal structure of the Fv corresponding to the anti-blood group A antibody AC1001 has been determined to 2.2-A resolution and reveals a binding pocket that is complementary to the blood group A-trisaccharide antigen. The effect of mutating specific residues lining this pocket on binding to the A and B blood group oligosaccharide antigens was investigated through a panel of single point mutations and through a phage library of mutations in complementarity determining region H3. Both approaches gave several mutants with improved affinity for antigen. Surface plasmon resonance indicated up to 8-fold enhancement in affinity for the A-pentasaccharide with no observable binding to the blood group B antigen. This is the first example of single point mutations in a carbohydrate-binding antibody resulting in significant increases in binding affinity without loss of specificity.
About this Structure
1JV5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of an anti-blood group A Fv and improvement of its binding affinity without loss of specificity., Thomas R, Patenaude SI, MacKenzie CR, To R, Hirama T, Young NM, Evans SV, J Biol Chem. 2002 Jan 18;277(3):2059-64. Epub 2001 Oct 25. PMID:11679577
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