Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NMC

COMPLEX BETWEEN NC10 ANTI-INFLUENZA VIRUS NEURAMINIDASE SINGLE CHAIN ANTIBODY WITH A 15 RESIDUE LINKER AND INFLUENZA VIRUS NEURAMINIDASE

1NMC の概要
エントリーDOI10.2210/pdb1nmc/pdb
分子名称NEURAMINIDASE, SINGLE CHAIN ANTIBODY, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
機能のキーワードcomplex (single-chain antibody-antigen), hydrolase, complex (single-chain antibody-antigen) complex, complex (single-chain antibody/antigen)
由来する生物種Influenza A virus
詳細
タンパク質・核酸の鎖数6
化学式量合計142042.49
構造登録者
Malby, R.L.,Mccoy, A.J.,Kortt, A.A.,Hudson, P.J.,Colman, P.M. (登録日: 1997-12-21, 公開日: 1998-09-23, 最終更新日: 2024-11-20)
主引用文献Malby, R.L.,McCoy, A.J.,Kortt, A.A.,Hudson, P.J.,Colman, P.M.
Three-dimensional structures of single-chain Fv-neuraminidase complexes.
J.Mol.Biol., 279:901-910, 1998
Cited by
PubMed Abstract: The structure of the complex between a recombinant single-chain Fv construct of antibody NC10 with a five-residue peptide linker between VH and VL (termed scFv(5)), and its antigen, tetrameric neuraminidase from influenza virus (NA), has been determined and refined at 2.5 A resolution. The antibody-antigen binding interface is very similar to that of a similar NC10 scFv-NA complex in which the scFv has a 15-residue peptide linker (scFv(15)), and the NC10 Fab-NA complex. However, scFv(5) and scFv(15) have different stoichiometries in solution. While scFv(15) is predominantly monomeric in solution, scFv(5) forms dimers exclusively, because the five-residue linker is not long enough to permit VH and VL domains from the same polypeptide associating and forming an antigen-binding site. Upon forming a complex with NA, scFv(15) forms a approximately 300 kDa complex corresponding to one NA tetramer binding four scFv(15) monomers, while scFv(5) forms a approximately 590 kDa complex, corresponding to two NA tetramers crosslinked by four bivalent scFv(5) dimers. However, the dimeric scFv(5) in the scFv(5)-NA crystals does not crosslink NA tetramers, and modelling studies indicate that it is not possible to pack four dimeric and simultaneously bivalent scFvs between the NA tetramers with only a five-residue linker between VH and VL. The inability arises from the exacting requirement to orient the two antigen-binding surfaces to bind the tetrameric NA antigen while avoiding steric clashes with NC10 scFv(5) dimers bound to other sites on the NA tetramer. The utility of bivalent or bifunctional scFvs with short linkers may therefore be restricted by the steric constraints imposed by binding multivalent antigens.
PubMed: 9642070
DOI: 10.1006/jmbi.1998.1794
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1nmc
検証レポート(詳細版)ダウンロードをダウンロード

238582

件を2025-07-09に公開中

PDB statisticsPDBj update infoContact PDBjnumon