1FOR

STRUCTURE DETERMINATION OF AN FAB FRAGMENT THAT NEUTRALIZES HUMAN RHINOVIRUS AND ANALYSIS OF THE FAB-VIRUS COMPLEX

1FOR の概要

• エントリーDOI: 10.2210/pdb1for/pdb
• 分子名称: IGG2A-KAPPA 17-IA FAB (LIGHT CHAIN), IGG2A-KAPPA 17-IA FAB (HEAVY CHAIN) (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: 2
• 化学式量合計: 46350.54

構造登録者

Smith, T.J.,Liu, H. (登録日: 1994-05-24, 公開日: 1994-09-30, 最終更新日: 2024-10-30)

主引用文献

Liu, H.,Smith, T.J.,Lee, W.M.,Mosser, A.G.,Rueckert, R.R.,Olson, N.H.,Cheng, R.H.,Baker, T.S.
Structure determination of an Fab fragment that neutralizes human rhinovirus 14 and analysis of the Fab-virus complex.
J.Mol.Biol., 240:127-137, 1994

PubMed Abstract: The crystal structure of Fab17-IA, an antigen-binding fragment from a murine immunoglobulin that neutralizes human rhinovirus 14 (HRV14), has been solved to 2.7 A resolution. Fab17-IA crystallized into three different space groups depending upon the method used to purify the intact antibody. The structure was determined by use of molecular and isomorphous replacement methods. The current model has a crystallographic R-factor of approximately 19% for 10,192 independent reflections between 8 and 2.7 A. Correlation coefficient calculations showed that the Fab17-IA structure can be fit into the Fab17-IA/HRV14 image reconstruction density to within 5 A positional accuracy and to within a few degrees of rotation. The resulting interface of the docked antibody was examined and showed extensive charge and shape complementarity with the virus surface that was supported by site-directed mutagenesis experiments. The success of this approach validates the utility of combining X-ray crystallography with cryo-electron microscopy of complex macromolecular assemblies.

PubMed: 8027997
DOI: 10.1006/jmbi.1994.1427

実験手法

X-RAY DIFFRACTION (2.75 Å)