1UAC

Crystal Structure of HYHEL-10 FV MUTANT SFSF Complexed with TURKEY WHITE LYSOZYME

1UAC の概要

• エントリーDOI: 10.2210/pdb1uac/pdb
• 分子名称: lysozyme binding Ig kappa chain V23-J2 region, Ig VH,anti-lysozyme, Lysozyme C, ... (4 entities in total)
• 機能のキーワード: antigen-antibody complex, hyhel-10, mutant, anti-lysozyme antibody, immune system-hydrolase complex, immune system/hydrolase
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Secreted: P00703
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 38615.85

構造登録者

Kumagai, I.,Nishimiya, Y.,Kondo, H.,Tsumoto, K. (登録日: 2003-03-08, 公開日: 2004-03-23, 最終更新日: 2024-11-20)

主引用文献

Kumagai, I.,Nishimiya, Y.,Kondo, H.,Tsumoto, K.
Structural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10
J.BIOL.CHEM., 278:24929-24936, 2003

PubMed Abstract: Decreased affinity of an antibody for a mutated epitope in an antigen can be enhanced and reversed by mutations in certain antibody residues. Here we describe the crystal structures of (a) the complex between a naturally mutated proteinaceous antigen and an antibody that was mutated and selected in vitro, and (b) the complex between the normal antigen and the mutated antibody. The mutated and selected antibody recognizes essentially the same epitope as in the wild-type antibody, indicating successful target site-directed functional alteration of the antibody. In comparing the structure of the mutated antigen-mutant antibody complex with the previously established structure of the wild-type antigen-wild-type antibody complex, we found that the enhanced affinity of the mutated antibody for the mutant antigen originated not from improvements in local complementarity around the mutated sites but from subtle and critical structural changes in nonmutated sites, including an increase in variable domain interactions. Our findings indicate that only a few mutations in the antigen-binding region of an antibody can lead to some structural changes in its paratopes, emphasizing the critical roles of the plasticity of loops in the complementarity-determining region and also the importance of the plasticity of the interaction between the variable regions of immunoglobulin heavy and light chains in determining the specificity of an antibody.

PubMed: 12709438
DOI: 10.1074/jbc.M301149200

実験手法

X-RAY DIFFRACTION (1.7 Å)