1C15

SOLUTION STRUCTURE OF APAF-1 CARD

1C15 の概要

• エントリーDOI: 10.2210/pdb1c15/pdb
• 関連するPDBエントリー: 1A1W 1DDF 3CRD
• NMR情報: BMRB: 4661
• 分子名称: APOPTOTIC PROTEASE ACTIVATING FACTOR 1 (1 entity in total)
• 機能のキーワード: programmed cell death, apaf, card, ded, dd, caspase recruitment domain, homophilic interaction, apoptosis
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O14727
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11099.71

構造登録者

Zhou, P.,Chou, J.,Olea, R.S.,Yuan, J.,Wagner, G. (登録日: 1999-07-20, 公開日: 1999-09-20, 最終更新日: 2024-05-22)

主引用文献

Zhou, P.,Chou, J.,Olea, R.S.,Yuan, J.,Wagner, G.
Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction.
Proc.Natl.Acad.Sci.USA, 96:11265-11270, 1999

PubMed Abstract: Direct recruitment and activation of caspase-9 by Apaf-1 through the homophilic CARD/CARD (Caspase Recruitment Domain) interaction is critical for the activation of caspases downstream of mitochondrial damage in apoptosis. Here we report the solution structure of the Apaf-1 CARD domain and its surface of interaction with caspase-9 CARD. Apaf-1 CARD consists of six tightly packed amphipathic alpha-helices and is topologically similar to the RAIDD CARD, with the exception of a kink observed in the middle of the N-terminal helix. By using chemical shift perturbation data, the homophilic interaction was mapped to the acidic surface of Apaf-1 CARD centered around helices 2 and 3. Interestingly, a significant portion of the chemically perturbed residues are hydrophobic, indicating that in addition to the electrostatic interactions predicted previously, hydrophobic interaction is also an important driving force underlying the CARD/CARD interaction. On the basis of the identified functional residues of Apaf-1 CARD and the surface charge complementarity, we propose a model of CARD/CARD interaction between Apaf-1 and caspase-9.

PubMed: 10500165
DOI: 10.1073/pnas.96.20.11265

実験手法

SOLUTION NMR