2B48

Bcl-XL 3D Domain Swapped Dimer

2B48 の概要

• エントリーDOI: 10.2210/pdb2b48/pdb
• 関連するPDBエントリー: 1MAZ 1R2D
• 分子名称: Apoptosis regulator Bcl-X (1 entity in total)
• 機能のキーワード: apoptosis, dimeric, 3d domain swap, alpha-helical, apoptosis inhibitor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform Bcl-X(L): Mitochondrion inner membrane : Q07817
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24606.94

構造登録者

O'Neill, J.W.,Manion, M.K.,Maguire, B.,Hockenbery, D.M. (登録日: 2005-09-22, 公開日: 2006-02-14, 最終更新日: 2023-08-23)

主引用文献

O'Neill, J.W.,Manion, M.K.,Maguire, B.,Hockenbery, D.M.
BCL-X(L) Dimerization by Three-dimensional Domain Swapping.
J.Mol.Biol., 356:367-381, 2006

PubMed Abstract: Dimeric interactions among anti- and pro-apoptotic members of the BCL-2 protein family are dynamically regulated and intimately involved in survival and death functions. We report the structure of a BCL-X(L) homodimers a 3D-domain swapped dimer (3DDS). The X-ray crystal structure demonstrates the mutual exchange of carboxy-terminal regions including BH2 (Bcl-2 homology 2) between monomer subunits, with the hinge region occurring at the hairpin turn between the fifth and sixth alpha helices. Both BH3 peptide-binding hydrophobic grooves are unoccupied in the 3DDS dimer and available for BH3 peptide binding, as confirmed by sedimentation velocity analysis. BCL-X(L) 3DDS dimers have increased pore-forming activity compared to monomers, suggesting that 3DDS dimers may act as intermediates in membrane pore formation. Chemical crosslinking studies of Cys-substituted BCL-X(L) proteins demonstrate that 3DDS dimers form in synthetic lipid vesicles.

PubMed: 16368107
DOI: 10.1016/j.jmb.2005.11.032

実験手法

X-RAY DIFFRACTION (3.45 Å)