1aj7

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(New page: 200px<br /> <applet load="1aj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aj7, resolution 2.1&Aring;" /> '''IMMUNOGLOBULIN 48G7 ...)
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'''IMMUNOGLOBULIN 48G7 GERMLINE FAB ANTIBODY COMPLEXED WITH HAPTEN 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID. AFFINITY MATURATION OF AN ESTEROLYTIC ANTIBODY'''<br />
'''IMMUNOGLOBULIN 48G7 GERMLINE FAB ANTIBODY COMPLEXED WITH HAPTEN 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID. AFFINITY MATURATION OF AN ESTEROLYTIC ANTIBODY'''<br />
==Overview==
==Overview==
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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.
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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==
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1AJ7 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] with NPE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AJ7 OCA].
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1AJ7 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] with <scene name='pdbligand=NPE:'>NPE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJ7 OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Patten, P.A.]]
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[[Category: Patten, P A.]]
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[[Category: Schultz, P.G.]]
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[[Category: Schultz, P G.]]
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[[Category: Stevens, R.C.]]
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[[Category: Stevens, R C.]]
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[[Category: Wang, L.H.]]
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[[Category: Wang, L H.]]
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[[Category: Wedemayer, G.J.]]
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[[Category: Wedemayer, G J.]]
[[Category: NPE]]
[[Category: NPE]]
[[Category: affinity maturation]]
[[Category: affinity maturation]]
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:59:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:04 2008''

Revision as of 09:45, 21 February 2008


1aj7, resolution 2.1Å

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IMMUNOGLOBULIN 48G7 GERMLINE FAB ANTIBODY COMPLEXED WITH HAPTEN 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID. 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

1AJ7 is a Protein complex structure of sequences from Homo sapiens and Mus musculus with as ligand. 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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