1AJ7

IMMUNOGLOBULIN 48G7 GERMLINE FAB ANTIBODY COMPLEXED WITH HAPTEN 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID. AFFINITY MATURATION OF AN ESTEROLYTIC ANTIBODY

1AJ7 の概要

• エントリーDOI: 10.2210/pdb1aj7/pdb
• 分子名称: IMMUNOGLOBULIN 48G7 FAB (LIGHT CHAIN), IMMUNOGLOBULIN 48G7 FAB (HEAVY CHAIN), 5-(PARA-NITROPHENYL PHOSPHONATE)-PENTANOIC ACID (3 entities in total)
• 機能のキーワード: germline antibody, fab, catalytic antibody, affinity maturation, immunoglobulin
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46829.93

構造登録者

Wedemayer, G.J.,Wang, L.H.,Patten, P.A.,Schultz, P.G.,Stevens, R.C. (登録日: 1997-05-15, 公開日: 1997-11-12, 最終更新日: 2024-10-09)

主引用文献

Wedemayer, G.J.,Patten, P.A.,Wang, L.H.,Schultz, P.G.,Stevens, R.C.
Structural insights into the evolution of an antibody combining site.
Science, 276:1665-1669, 1997

PubMed Abstract: 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.

PubMed: 9180069
DOI: 10.1126/science.276.5319.1665

実験手法

X-RAY DIFFRACTION (2.1 Å)