1CY5

CRYSTAL STRUCTURE OF THE APAF-1 CARD

Summary for 1CY5

• Entry DOI: 10.2210/pdb1cy5/pdb
• Descriptor: PROTEIN (APOPTOTIC PROTEASE ACTIVATING FACTOR 1), ZINC ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• Functional Keywords: caspase recruitment domain, death fold, six alpha-helix bundle, greek key topology, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : O14727
• Total number of polymer chains: 1
• Total formula weight: 11504.89

Authors

Vaughn, D.E.,Joshua-Tor, L. (deposition date: 1999-08-31, release date: 1999-09-13, Last modification date: 2025-03-26)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.3 Å)