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| - | [[Image:1p2c.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1p2c.png|left|200px]] |
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| | {{STRUCTURE_1p2c| PDB=1p2c | SCENE= }} | | {{STRUCTURE_1p2c| PDB=1p2c | SCENE= }} |
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| - | '''crystal structure analysis of an anti-lysozyme antibody'''
| + | ===crystal structure analysis of an anti-lysozyme antibody=== |
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| - | ==Overview==
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| - | In the immune response against a typical T cell-dependent protein antigen, the affinity maturation process is fast and is associated with the early class switch from IgM to IgG. As such, a comprehension of the molecular basis of affinity maturation could be of great importance in biomedical and biotechnological applications. Affinity maturation of anti-protein antibodies has been reported to be the result of small structural changes, mostly confined to the periphery of the antigen-combining site. However, little is understood about how these small structural changes account for the increase in the affinity toward the antigen. Herein, we present the three-dimensional structure of the Fab fragment from BALB/c mouse mAb F10.6.6 in complex with the antigen lysozyme. This antibody was obtained from a long-term exposure to the antigen. mAb F10.6.6, and the previously described antibody D44.1, are the result of identical or nearly identical somatic recombination events. However, different mutations in the framework and variable regions result in an approximately 10(3) higher affinity for the F10.6.6 antibody. The comparison of the three-dimensional structures of these Fab-lysozyme complexes reveals that the affinity maturation produces a fine tuning of the complementarity of the antigen-combining site toward the epitope, explaining at the molecular level how the immune system is able to increase the affinity of an anti-protein antibody to subnanomolar levels.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14988501}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14988501 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14988501}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Kappa antibody/antigen complex]] | | [[Category: Kappa antibody/antigen complex]] |
| | [[Category: Monoclonal antibody igg1]] | | [[Category: Monoclonal antibody igg1]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:35:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:53:46 2008'' |
Revision as of 03:53, 29 July 2008
Template:STRUCTURE 1p2c
crystal structure analysis of an anti-lysozyme antibody
Template:ABSTRACT PUBMED 14988501
About this Structure
1P2C is a Single protein structure of sequence from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural mechanism for affinity maturation of an anti-lysozyme antibody., Cauerhff A, Goldbaum FA, Braden BC, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3539-44. Epub 2004 Feb 26. PMID:14988501
Page seeded by OCA on Tue Jul 29 06:53:46 2008
