2DQI

Crystal structure of hyhel-10 FV mutant (Ly50a) complexed with hen egg lysozyme

2DQI の概要

• エントリーDOI: 10.2210/pdb2dqi/pdb
• 関連するPDBエントリー: 1C08 2DQC 2DQD 2DQE 2DQF 2DQG 2DQH 2DQJ
• 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, mutant, 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: 38658.81

構造登録者

Shiroishi, M.,Kondo, H.,Tsumoto, K.,Kumagai, I. (登録日: 2006-05-26, 公開日: 2007-01-23, 最終更新日: 2024-10-23)

主引用文献

Shiroishi, M.,Tsumoto, K.,Tanaka, Y.,Yokota, A.,Nakanishi, T.,Kondo, H.,Kumagai, I.
Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL
J.Biol.Chem., 282:6783-6791, 2007

PubMed Abstract: Tyrosine is an important amino acid in protein-protein interaction hot spots. In particular, many Tyr residues are located in the antigen-binding sites of antibodies and endow high affinity and high specificity to these antibodies. To investigate the role of interfacial Tyr residues in protein-protein interactions, we performed crystallographic studies and thermodynamic analyses of the interaction between hen egg lysozyme (HEL) and the anti-HEL antibody HyHEL-10 Fv fragment. HyHEL-10 has six Tyr residues in its antigen-binding site, which were systematically mutated to Phe and Ala using site-directed mutagenesis. The crystal structures revealed several critical roles for these Tyr residues in the interaction between HEL and HyHEL-10 as follows: 1) the aromatic ring of Tyr-50 in the light chain (LTyr-50) was important for the correct ternary structure of variable regions of the immunoglobulin light chain and heavy chain and of HEL; 2) deletion of the hydroxyl group of Tyr-50 in the heavy chain (HTyr-50) resulted in structural changes in the antigen-antibody interface; and 3) the side chains of HTyr-33 and HTyr-53 may help induce fitting of the antibody to the antigen. Hot spot Tyr residues may contribute to the high affinity and high specificity of the antigen-antibody interaction through a diverse set of structural and thermodynamic interactions.

PubMed: 17166830
DOI: 10.1074/jbc.M605197200

実験手法

X-RAY DIFFRACTION (2 Å)