5FCG

Crystal structure of Bcl-2 in complex with HBx-BH3 motif

5FCG の概要

• エントリーDOI: 10.2210/pdb5fcg/pdb
• 分子名称: Apoptosis regulator Bcl-2, Protein X (3 entities in total)
• 機能のキーワード: complex, apoptosis
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22603.28

構造登録者

Jiang, T.Y.,Liu, M.H.,Wu, J.P.,Shi, Y.G. (登録日: 2015-12-15, 公開日: 2016-02-10, 最終更新日: 2023-11-08)

主引用文献

Jiang, T.Y.,Liu, M.H.,Wu, J.P.,Shi, Y.G.
Structural and biochemical analysis of Bcl-2 interaction with the hepatitis B virus protein HBx
Proc.Natl.Acad.Sci.USA, 2016

PubMed Abstract: HBx is a hepatitis B virus protein that is required for viral infectivity and replication. Anti-apoptotic Bcl-2 family members are thought to be among the important host targets of HBx. However, the structure and function of HBx are poorly understood and the molecular mechanism of HBx-induced carcinogenesis remains unknown. In this study, we report biochemical and structural characterization of HBx. The recombinant HBx protein contains metal ions, in particular iron and zinc. A BH3-like motif in HBx (residues 110-135) binds Bcl-2 with a dissociation constant of ∼193 μM, which is drastically lower than that for a canonical BH3 motif from Bim or Bad. Structural analysis reveals that, similar to other BH3 motifs, the BH3-like motif of HBx adopts an amphipathic α-helix and binds the conserved BH3-binding groove on Bcl-2. Unlike the helical Bim or Bad BH3 motif, the C-terminal portion of the bound HBx BH3-like motif has an extended conformation and makes considerably fewer interactions with Bcl-2. These observations suggest that HBx may modulate Bcl-2 function in a way that is different from that of the classical BH3-only proteins.

PubMed: 26858413
DOI: 10.1073/pnas.1525616113

実験手法

X-RAY DIFFRACTION (2.1 Å)