1AF3

RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN

1AF3 の概要

• エントリーDOI: 10.2210/pdb1af3/pdb
• 分子名称: APOPTOSIS REGULATOR BCL-X (2 entities in total)
• 機能のキーワード: bcl-xl, apoptosis, mitochondrion, alternative splicing, regulatory protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Isoform Bcl-X(L): Mitochondrion inner membrane: P53563
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22082.25

構造登録者

Aritomi, M.,Kunishima, N.,Inohara, N.,Ishibashi, Y.,Ohta, S.,Morikawa, K. (登録日: 1997-03-21, 公開日: 1997-07-07, 最終更新日: 2024-02-07)

主引用文献

Aritomi, M.,Kunishima, N.,Inohara, N.,Ishibashi, Y.,Ohta, S.,Morikawa, K.
Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family.
J.Biol.Chem., 272:27886-27892, 1997

PubMed Abstract: Bcl-xL is a member of the Bcl-2 protein family, which regulates apoptosis. Preparation of recombinant rat Bcl-xL yielded two forms, one deamidated at -Asn-Gly- sequences to produce isoaspartates and the other not deamidated. The crystal structures of the two forms show that they both adopt an essentially identical backbone structure which resembles the fold of human Bcl-xL: three layers of two alpha-helices each, capped at one end by two short helices. Both forms have a long disordered region, which contains the potential deamidation sites. The molecular structure exhibits a low level of interhelical interactions, the presence of three cavities, and a notable hydrophobic cleft surrounded by walls rich in basic residues. These unique structural features may be favorable for its accommodation into membranes or for possible rearrangement to modulate homo-/heterodimerization. Homology modeling of Bcl-2 and Bax, based on the Bcl-xL structure, suggests that Bax has the strongest potential for membrane insertion. Furthermore, we found a possible interface for interaction with non-Bcl-2 family member proteins, such as CED-4 homologues.

PubMed: 9346936
DOI: 10.1074/jbc.272.44.27886

実験手法

X-RAY DIFFRACTION (2.5 Å)