2rcs
From Proteopedia
(New page: 200px<br /> <applet load="2rcs" size="450" color="white" frame="true" align="right" spinBox="true" caption="2rcs, resolution 2.1Å" /> '''IMMUNOGLOBULIN 48G7 ...) |
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| - | [[Image:2rcs.gif|left|200px]]<br /> | + | [[Image:2rcs.gif|left|200px]]<br /><applet load="2rcs" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2rcs" size=" | + | |
caption="2rcs, resolution 2.1Å" /> | caption="2rcs, resolution 2.1Å" /> | ||
'''IMMUNOGLOBULIN 48G7 GERMLINE FAB-AFFINITY MATURATION OF AN ESTEROLYTIC ANTIBODY'''<br /> | '''IMMUNOGLOBULIN 48G7 GERMLINE FAB-AFFINITY MATURATION OF AN ESTEROLYTIC ANTIBODY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of a germline antibody Fab fragment and its complex | + | The crystal structures of a germline antibody Fab fragment and its complex with hapten have been solved at 2.1 A resolution. These structures are compared with the corresponding crystal structures of the affinity-matured antibody, 48G7, which has a 30,000 times higher affinity for hapten as a result of nine replacement somatic mutations. Significant changes in the configuration of the combining site occur upon binding of hapten to the germline antibody, whereas hapten binds to the mature antibody by a lock-and-key fit mechanism. The reorganization of the combining site that was nucleated by hapten binding is further optimized by somatic mutations that occur up to 15 from bound hapten. These results suggest that the binding potential of the primary antibody repertoire may be significantly expanded by the ability of germline antibodies to adopt more than one combining-site configuration, with both antigen binding and somatic mutation stabilizing the configuration with optimal hapten complementarity. |
==About this Structure== | ==About this Structure== | ||
| - | 2RCS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 2RCS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Patten, P | + | [[Category: Patten, P A.]] |
| - | [[Category: Schultz, P | + | [[Category: Schultz, P G.]] |
| - | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
| - | [[Category: Wang, L | + | [[Category: Wang, L H.]] |
| - | [[Category: Wedemayer, G | + | [[Category: Wedemayer, G J.]] |
[[Category: affinity maturation]] | [[Category: affinity maturation]] | ||
[[Category: catalytic antibody]] | [[Category: catalytic antibody]] | ||
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[[Category: germline antibody]] | [[Category: germline antibody]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:46:14 2008'' |
Revision as of 16:46, 21 February 2008
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IMMUNOGLOBULIN 48G7 GERMLINE FAB-AFFINITY MATURATION OF AN ESTEROLYTIC ANTIBODY
Overview
The crystal structures of a germline antibody Fab fragment and its complex with hapten have been solved at 2.1 A resolution. These structures are compared with the corresponding crystal structures of the affinity-matured antibody, 48G7, which has a 30,000 times higher affinity for hapten as a result of nine replacement somatic mutations. Significant changes in the configuration of the combining site occur upon binding of hapten to the germline antibody, whereas hapten binds to the mature antibody by a lock-and-key fit mechanism. The reorganization of the combining site that was nucleated by hapten binding is further optimized by somatic mutations that occur up to 15 from bound hapten. These results suggest that the binding potential of the primary antibody repertoire may be significantly expanded by the ability of germline antibodies to adopt more than one combining-site configuration, with both antigen binding and somatic mutation stabilizing the configuration with optimal hapten complementarity.
About this Structure
2RCS is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural insights into the evolution of an antibody combining site., Wedemayer GJ, Patten PA, Wang LH, Schultz PG, Stevens RC, Science. 1997 Jun 13;276(5319):1665-9. PMID:9180069
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