1LXL

NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE

1LXL の概要

• エントリーDOI: 10.2210/pdb1lxl/pdb
• 分子名称: BCL-XL (1 entity in total)
• 機能のキーワード: apoptosis, programmed cell death, bcl-2 family
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Mitochondrion membrane; Single-pass membrane protein (By similarity): Q07817
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24879.37

構造登録者

Muchmore, S.W.,Sattler, M.,Liang, H.,Meadows, R.P.,Harlan, J.E.,Yoon, H.S.,Nettesheim, D.,Chang, B.S.,Thompson, C.B.,Wong, S.L.,Ng, S.C.,Fesik, S.W. (登録日: 1996-04-04, 公開日: 1997-04-21, 最終更新日: 2024-05-22)

主引用文献

Muchmore, S.W.,Sattler, M.,Liang, H.,Meadows, R.P.,Harlan, J.E.,Yoon, H.S.,Nettesheim, D.,Chang, B.S.,Thompson, C.B.,Wong, S.L.,Ng, S.L.,Fesik, S.W.
X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.
Nature, 381:335-341, 1996

PubMed Abstract: THE Bcl-2 family of proteins regulate programmed cell death by an unknown mechanism. Here we describe the crystal and solution structures of a Bcl-2 family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic alpha-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices alpha1 and alpha2 was found to be flexible and non-essential for anti-apoptotic activity. The three functionally important Bcl-2 homology regions (BH1, BH2 and BH3) are in close spatial proximity and form an elongated hydrophobic cleft that may represent the binding site for other Bcl-2 family members. The arrangement of the alpha-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphtheria toxin and the colicins. The structural similarity may provide a clue to the mechanism of action of the Bcl-2 family of proteins.

PubMed: 8692274
DOI: 10.1038/381335a0

実験手法

SOLUTION NMR