1IGJ

26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY

1IGJ の概要

• エントリーDOI: 10.2210/pdb1igj/pdb
• 分子名称: IGG2A-KAPPA 26-10 FAB (LIGHT CHAIN), IGG2A-KAPPA 26-10 FAB (HEAVY CHAIN), DIGOXIN (3 entities in total)
• 機能のキーワード: immunoglobulin
• 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: 96291.28

構造登録者

Jeffrey, P.D.,Sheriff, S. (登録日: 1993-02-19, 公開日: 1993-04-15, 最終更新日: 2024-10-16)

主引用文献

Jeffrey, P.D.,Strong, R.K.,Sieker, L.C.,Chang, C.Y.,Campbell, R.L.,Petsko, G.A.,Haber, E.,Margolies, M.N.,Sheriff, S.
26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity.
Proc.Natl.Acad.Sci.USA, 90:10310-10314, 1993

PubMed Abstract: We have determined the three-dimensional structures of the antigen-binding fragment of the anti-digoxin monoclonal antibody 26-10 in the uncomplexed state at 2.7 A resolution and as a complex with digoxin at 2.5 A resolution. Neither the antibody nor digoxin undergoes any significant conformational changes upon forming the complex. Digoxin interacts primarily with the antibody heavy chain and is oriented such that the carbohydrate groups are exposed to solvent and the lactone ring is buried in a deep pocket at the bottom of the combining site. Despite extensive interactions between antibody and antigen, no hydrogen bonds or salt links are formed between 26-10 and digoxin. Thus the 26-10-digoxin complex is unique among the known three-dimensional structures of antibody-antigen complexes in that specificity and high affinity arise primarily from shape complementarity.

PubMed: 8234291
DOI: 10.1073/pnas.90.21.10310

実験手法

X-RAY DIFFRACTION (2.5 Å)