1CY5

CRYSTAL STRUCTURE OF THE APAF-1 CARD

1CY5 の概要

• エントリーDOI: 10.2210/pdb1cy5/pdb
• 分子名称: PROTEIN (APOPTOTIC PROTEASE ACTIVATING FACTOR 1), ZINC ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: caspase recruitment domain, death fold, six alpha-helix bundle, greek key topology, 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: 11504.89

構造登録者

Vaughn, D.E.,Joshua-Tor, L. (登録日: 1999-08-31, 公開日: 1999-09-13, 最終更新日: 2025-03-26)

主引用文献

Vaughn, D.E.,Rodriguez, J.,Lazebnik, Y.,Joshua-Tor, L.
Crystal structure of Apaf-1 caspase recruitment domain: an alpha-helical Greek key fold for apoptotic signaling.
J.Mol.Biol., 293:439-447, 1999

PubMed Abstract: The caspase recruitment domain (CARD) of Apaf-1 binds to the CARD of caspase-9 to trigger a proteolytic cascade that leads to apoptotic cell death. We report the crystal structure of the Apaf-1 CARD at 1. 3 A resolution, solved in a two-element multiwavelength anomalous dispersion (MAD) X-ray diffraction experiment. This CARD adopts a six-helix bundle fold with Greek key topology surrounding an extensive hydrophobic core. This fold, which we call the "death fold", is found in other domains that mediate interactions in apoptotic signaling despite very low sequence identity. From a structure-based alignment, we identify conserved patterns that characterize the death fold and its subclasses. Like the Ig-fold, it provides a rigid structural scaffold upon which diverse recognition surfaces are assembled.

PubMed: 10543941
DOI: 10.1006/jmbi.1999.3177

実験手法

X-RAY DIFFRACTION (1.3 Å)