1Q59

Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2

1Q59 の概要

• エントリーDOI: 10.2210/pdb1q59/pdb
• 分子名称: Early antigen protein R (1 entity in total)
• 機能のキーワード: bhrf1, bcl-2, epstein-barr virus, nmr spectroscopy, structure determination, viral protein
• 由来する生物種: Human herpesvirus 4 (Epstein-Barr virus)
• 細胞内の位置: Host membrane; Single-pass membrane protein (Potential): P03182
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19848.25

構造登録者

Huang, Q.,Petros, A.M.,Virgin, H.W.,Fesik, S.W.,Olejniczak, E.T. (登録日: 2003-08-06, 公開日: 2003-09-23, 最終更新日: 2024-05-22)

主引用文献

Huang, Q.,Petros, A.M.,Virgin, H.W.,Fesik, S.W.,Olejniczak, E.T.
Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
J.Mol.Biol., 332:1123-1130, 2003

PubMed Abstract: 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.

PubMed: 14499614
DOI: 10.1016/j.jmb.2003.08.007

実験手法

SOLUTION NMR