1J1X

Crystal Structure of HyHEL-10 Fv mutant LS93A complexed with hen egg white lysozyme

1J1X の概要

• エントリーDOI: 10.2210/pdb1j1x/pdb
• 関連するPDBエントリー: 1C08 1J1O 1J1P
• 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, 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: P00698
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 38734.91

構造登録者

Yokota, A.,Tsumoto, K.,Shiroishi, M.,Kondo, H.,Kumagai, I. (登録日: 2002-12-20, 公開日: 2003-01-14, 最終更新日: 2024-11-20)

主引用文献

Yokota, A.,Tsumoto, K.,Shiroishi, M.,Kondo, H.,Kumagai, I.
The Role of Hydrogen Bonding via Interfacial Water Molecules in Antigen-Antibody Complexation. THE HyHEL-10-HEL INTERACTION
J.BIOL.CHEM., 278:5410-5418, 2003

PubMed Abstract: To study the role of hydrogen bonding via interfacial water molecules in protein-protein interactions, we examined the interaction between hen egg white lysozyme (HEL) and its HyHEL-10 variable domain fragment (Fv) antibody. We constructed three antibody mutants (l-Y50F, l-S91A, and l-S93A) and investigated the interactions between the mutant Fvs and HEL. Isothermal titration calorimetry indicated that the mutations significantly decreased the negative enthalpy change (8-25 kJ mol(-1)), despite some offset by a favorable entropy change. X-ray crystallography demonstrated that the complexes had nearly identical structures, including the positions of the interfacial water molecules. Taken together, the isothermal titration calorimetric and x-ray crystallographic results indicate that hydrogen bonding via interfacial water enthalpically contributes to the Fv-HEL interaction despite the partial offset because of entropy loss, suggesting that hydrogen bonding stiffens the antigen-antibody complex.

PubMed: 12444085
DOI: 10.1074/jbc.M210182200

実験手法

X-RAY DIFFRACTION (1.8 Å)