2Q76

Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment

2Q76 の概要

• エントリーDOI: 10.2210/pdb2q76/pdb
• 関連するPDBエントリー: 1MLB 1MLC 1P2C
• 分子名称: Fab F10.6.6 fragment Light Chain, Fab F10.6.6 fragment Heavy Chain (3 entities in total)
• 機能のキーワード: antibody, fab fragment, lysozyme, affinity maturation, vh-vl interface., immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93038.87

構造登録者

Cauerhff, A.,Klinke, S.,Acierno, J.P.,Goldbaum, F.A.,Braden, B.C. (登録日: 2007-06-06, 公開日: 2008-03-18, 最終更新日: 2024-10-09)

主引用文献

Acierno, J.P.,Braden, B.C.,Klinke, S.,Goldbaum, F.A.,Cauerhff, A.
Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies.
J.Mol.Biol., 374:130-146, 2007

PubMed Abstract: The somatic mutations accumulated in variable and framework regions of antibodies produce structural changes that increase the affinity towards the antigen. This implies conformational and non covalent bonding changes at the paratope, as well as possible quaternary structure changes and rearrangements at the V(H)-V(L) interface. The consequences of the affinity maturation on the stability of the Fv domain were studied in a system composed of two closely related antibodies, F10.6.6 and D44.1, which recognize the same hen egg-white lysozyme (HEL) epitope. The mAb F10.6.6 has an affinity constant 700 times higher than D44.1, due to a higher surface complementarity to HEL. The structure of the free form of the Fab F10.6.6 presented here allows a comparative study of the conformational changes produced upon binding to antigen. By means of structural comparison, kinetics and thermodynamics of binding and stability studies on Fab and Fv fragments of both antibodies, we have determined that the affinity maturation process of anti-protein antibodies affects the shape of the combining site and the secondary structure content of the variable domain, stabilizes the V(H)-V(L) interaction, and consequently produces an increase of the Fv domain stability, improving the binding to antigen.

PubMed: 17916365
DOI: 10.1016/j.jmb.2007.09.005

実験手法

X-RAY DIFFRACTION (2 Å)