3V6A

Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules

3V6A の概要

• エントリーDOI: 10.2210/pdb3v6a/pdb
• 関連するPDBエントリー: 3U0R
• 分子名称: Apoptosis inhibitor 5 (2 entities in total)
• 機能のキーワード: heat and armadillo-like repeat, fgf-2, acinus, nucleus, apoptosis inhibitor
• 由来する生物種: Homo sapiens
• 細胞内の位置: Nucleus. Isoform 3: Cytoplasm: Q9BZZ5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53587.36

構造登録者

Lee, B.I.,Han, B.G.,Lee, S.J. (登録日: 2011-12-19, 公開日: 2012-02-22, 最終更新日: 2023-11-08)

主引用文献

Han, B.G.,Kim, K.H.,Lee, S.J.,Jeong, K.C.,Cho, J.W.,Noh, K.H.,Kim, T.W.,Kim, S.J.,Yoon, H.J.,Suh, S.W.,Lee, S.H.,Lee, B.I.
Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules.
J.Biol.Chem., 287:10727-10737, 2012

PubMed Abstract: Apoptosis inhibitor 5 (API5) is an anti-apoptotic protein that is up-regulated in various cancer cells. Here, we present the crystal structure of human API5. API5 exhibits an elongated all α-helical structure. The N-terminal half of API5 is similar to the HEAT repeat and the C-terminal half is similar to the ARM (Armadillo-like) repeat. HEAT and ARM repeats have been implicated in protein-protein interactions, suggesting that the cellular roles of API5 may be to mediate protein-protein interactions. Various components of multiprotein complexes have been identified as API5-interacting protein partners, suggesting that API5 may act as a scaffold for multiprotein complexes. API5 exists as a monomer, and the functionally important heptad leucine repeat does not exhibit the predicted a dimeric leucine zipper. Additionally, Lys-251, which can be acetylated in cells, plays important roles in the inhibition of apoptosis under serum deprivation conditions. The acetylation of this lysine also affects the stability of API5 in cells.

PubMed: 22334682
DOI: 10.1074/jbc.M111.317594

実験手法

X-RAY DIFFRACTION (2.6 Å)