1p2c
From Proteopedia
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crystal structure analysis of an anti-lysozyme antibody
Overview
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.
About this Structure
1P2C is a Single protein structure of sequence from Gallus gallus and Mus musculus. Active as Lysozyme, with EC number 3.2.1.17 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
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