1QGC

STRUCTURE OF THE COMPLEX OF A FAB FRAGMENT OF A NEUTRALIZING ANTIBODY WITH FOOT AND MOUTH DISEASE VIRUS

1QGC の概要

• エントリーDOI: 10.2210/pdb1qgc/pdb
• 分子名称: PROTEIN (VIRUS CAPSID PROTEIN VP1), PROTEIN (VIRUS CAPSID PROTEIN VP2), PROTEIN (VIRUS CAPSID PROTEIN VP3), ... (6 entities in total)
• 機能のキーワード: virus-antibody complex, icosahedral virus, virus-immune system complex, virus/immune system
• 由来する生物種: Foot-and-mouth disease virus - type C; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 120905.43

構造登録者

Fita, I. (登録日: 1999-04-23, 公開日: 2000-01-26, 最終更新日: 2023-12-27)

主引用文献

Hewat, E.A.,Verdaguer, N.,Fita, I.,Blakemore, W.,Brookes, S.,King, A.,Newman, J.,Domingo, E.,Mateu, M.G.,Stuart, D.I.
Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop.
EMBO J., 16:1492-1500, 1997

PubMed Abstract: Data from cryo-electron microscopy and X-ray crystallography have been combined to study the interactions of foot-and-mouth disease virus serotype C (FMDV-C) with a strongly neutralizing monoclonal antibody (mAb) SD6. The mAb SD6 binds to the long flexible GH-loop of viral protein 1 (VP1) which also binds to an integrin receptor. The structure of the virus-Fab complex was determined to 30 A resolution using cryo-electron microscopy and image analysis. The known structure of FMDV-C, and of the SD6 Fab co-crystallized with a synthetic peptide corresponding to the GH-loop of VP1, were fitted to the cryo-electron microscope density map. The SD6 Fab is seen to project almost radially from the viral surface in an orientation which is only compatible with monovalent binding of the mAb. Even taking into account the mAb hinge and elbow flexibility, it is not possible to model bivalent binding without severely distorting the Fabs. The bound GH-loop is essentially in what has previously been termed the 'up' position in the best fit Fab orientation. The SD6 Fab interacts almost exclusively with the GH-loop of VP1, making very few other contacts with the viral capsid. The position and orientation of the SD6 Fab bound to FMDV-C is in accord with previous immunogenic data.

PubMed: 9130694
DOI: 10.1093/emboj/16.7.1492

実験手法

ELECTRON MICROSCOPY (30 Å)