Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2
Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2
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DOI：
10.1016/j.jmb.2003.08.007
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发表时间：
2003-10-03
影响因子：
5.6
通讯作者：
Olejniczak, ET
中科院分区：
文献类型：
--
作者：
Huang, QL;Petros, AM;Olejniczak, ET
BHRF 1，Bcl-2同系物从EB病毒（EBV），已确定的三维结构的NMR光谱。虽然整体结构与其他Bcl-2家族成员相似，但存在重要的结构差异。与其他一些Bcl-2家族成员不同，BHRF 1不包含介导与促凋亡家族成员结合的突出疏水沟。此外，与抗凋亡Bcl-2蛋白相反，BHRF 1不与衍生自促凋亡蛋白巴克、Bax、Bik和Bad的肽紧密结合。在BHRF 1中缺乏暴露的、预先形成的结合沟，以及缺乏与衍生自结合其它抗凋亡家族成员的促凋亡家族成员的肽的显著结合，表明BHRF 1抗凋亡活性的机制与细胞Bcl-x（L）或Bcl-2的机制不平行。(C)2003 Elsevier Ltd.保留所有权利。
The three-dimensional structure of BHRF1, the Bcl-2 homolog from Epstein-Barr virus (EBV), has been determined by NMR spectroscopy. Although the overall structure is similar to other Bcl-2 family members, there are important structural differences. Unlike some of the other Bcl-2 family members, BHRF1 does not contain the prominent hydrophobic groove that mediates binding to pro-apoptotic family members. In addition, in contrast to the anti-apoptotic Bcl-2 proteins, BHRF1 does not bind tightly to peptides derived from the pro-apoptotic proteins Bak, Bax, Bik, and Bad. The lack of an exposed, pre-formed binding groove in BHRF1 and the lack of significant binding to peptides derived from pro-apoptotic family members that bind to other anti-apoptotic family members, suggest that the mechanism of the BHRF1 anti-apoptotic activity does not parallel that of cellular Bcl-x(L) or Bcl-2. (C) 2003 Elsevier Ltd. All rights reserved.