2F19
THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY
「1F19」から置き換えられました2F19 の概要
| エントリーDOI | 10.2210/pdb2f19/pdb |
| 関連するPDBエントリー | 1FAI |
| 分子名称 | IGG2B-KAPPA R19.9 FAB (LIGHT CHAIN), IGG2B-KAPPA R19.9 FAB (HEAVY CHAIN) (2 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 | 2 |
| 化学式量合計 | 47256.36 |
| 構造登録者 | Lascombe, M.B.,Alzari, P.M.,Poljak, R.J.,Nisonoff, A. (登録日: 1992-05-27, 公開日: 1992-10-15, 最終更新日: 2024-11-13) |
| 主引用文献 | Lascombe, M.-B.,Alzari, P.M.,Poljak, R.J.,Nisonoff, A. Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody. Proc.Natl.Acad.Sci.USA, 89:9429-9433, 1992 Cited by PubMed Abstract: The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site. PubMed: 1409652DOI: 10.1073/pnas.89.20.9429 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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