1N64

Crystal structure analysis of the immunodominant antigenic site on Hepatitis C virus protein bound to mAb 19D9D6

1N64 の概要

• エントリーDOI: 10.2210/pdb1n64/pdb
• 分子名称: Fab 19D9D6 light chain, Fab 19D9D6 heavy chain, Genome polyprotein Capsid protein C, ... (4 entities in total)
• 機能のキーワード: antibody peptide complex, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P29846
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 49538.41

構造登録者

Menez, R.,Bossus, M.,Muller, B.,Sibai, G.,Dalbon, P.,Ducancel, F.,Jolivet-Reynaud, C.,Stura, E. (登録日: 2002-11-08, 公開日: 2003-02-25, 最終更新日: 2024-11-13)

主引用文献

Menez, R.,Bossus, M.,Muller, B.H.,Sibai, G.,Dalbon, P.,Ducancel, F.,Jolivet-Reynaud, C.,Stura, E.A.
Crystal structure of a hydrophobic immunodominant antigenic site on hepatitis C virus core protein complexed to monoclonal antibody 19D9D6.
J.Immunol., 170:1917-1924, 2003

PubMed Abstract: The first crystal structure of a complex between a hepatitis C virus (HCV) core protein-derived peptide (residues 13-40) and the Ab fragment of a murine mAb (19D9D6) has been solved, allowing determination of the recognized epitope and elucidation of its conformation. This Ab, raised against the first 120 residues of the core protein, recognizes core particles and strongly competes with anticore human Abs, suggesting that it is highly representative of the human anti-HCV core response. Its epitope lies within the first 45 aa of the protein, the major antigenic segment of core recognized both by murine and human Abs. Surprisingly, the recognized epitope (29-37: QIVGGVYLL) has an unusual preponderance of hydrophobic residues, some of which are buried in a small hydrophobic core in the nuclear magnetic resonance structure of the peptide (2-45) in solution, suggesting that the Ab may induce a structural rearrangement upon recognition. The flexibility may reside entirely within the Ag, since the Fab'-peptide complex structure at 2.34 A shows that the Ab binding site is hardly perturbed by complexation. Given that the recognized residues are unlikely to be solvent exposed, we are left with the interesting possibility that Ab-core interactions may take place in a nonaqueous environment.

PubMed: 12574359

実験手法

X-RAY DIFFRACTION (2.34 Å)