1NLD

FAB FRAGMENT OF A NEUTRALIZING ANTIBODY DIRECTED AGAINST AN EPITOPE OF GP41 FROM HIV-1

1NLD の概要

• エントリーDOI: 10.2210/pdb1nld/pdb
• 分子名称: FAB1583 (2 entities in total)
• 機能のキーワード: fab fragment, 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: 47146.61

構造登録者

Davies, C.,Beauchamp, J.C.,Emery, D.,Rawas, A.,Muirhead, H. (登録日: 1996-07-02, 公開日: 1996-12-23, 最終更新日: 2024-10-09)

主引用文献

Davies, C.,Beauchamp, J.C.,Emery, D.,Rawas, A.,Muirhead, H.
Structure of the Fab fragment from a neutralizing monoclonal antibody directed against an epitope of gp41 from HIV-1.
Acta Crystallogr.,Sect.D, 53:186-194, 1997

PubMed Abstract: The structure of a Fab fragment of a monoclonal antibody (1583) that neutralizes a broad range of HIV-1 isolates has been solved by X-ray crystallography. This antibody is directed against a poliovirus/HIV-I chimaera which presents a conserved epitope of the envelope protein gp41. Crystals of 1583 were obtained in the space group P2(1)2(1)2(1) and the structure solved by molecular replacement. The model has been refined against all data in the range 10-2.9 A to a final crystallographic R factor of 0.198. The antigen-binding site features a well defined groove, typical of antibodies that bind to small antigens, created in part by a relatively short CDR H3. The variable regions of 1583 were sequenced and, given the hydrophilic nature of the epitope, revealed a surprising lack of charged residues in the CDR's. However, the antigen-binding cleft is indeed very polar, due in part to the presence of two charged residues that emanate from outside the recognized CDR's.

PubMed: 15299953
DOI: 10.1107/S0907444996012048

実験手法

X-RAY DIFFRACTION (2.9 Å)