Apoptotic peptidase activating factor 1

1C15, 1CWW, 1CY5, 1Z6T, 2P1H, 2YGS, 3J2T, 3YGS, 4RHW, 3JBT31711783ENSG00000120868ENSMUSG00000019979O14727O88879NM_001160NM_013229NM_181861NM_181868NM_181869NM_001042558NM_001282947NM_009684NP_001151NP_037361NP_863651NP_863658NP_863659NP_001036023NP_001269876NP_033814Apoptotic protease activating factor 1, also known as APAF1, is a human homolog of C. elegans CED-4 gene.1c15: SOLUTION STRUCTURE OF APAF-1 CARD1cww: SOLUTION STRUCTURE OF THE CASPASE RECRUITMENT DOMAIN (CARD) FROM APAF-11cy5: CRYSTAL STRUCTURE OF THE APAF-1 CARD1z6t: Structure of the apoptotic protease-activating factor 1 bound to ADP2p1h: Rapid Folding and Unfolding of Apaf-1 CARD2ygs: CARD DOMAIN FROM APAF-13ygs: APAF-1 CARD IN COMPLEX WITH PRODOMAIN OF PROCASPASE-9 Apoptotic protease activating factor 1, also known as APAF1, is a human homolog of C. elegans CED-4 gene. This gene encodes a cytoplasmic protein that forms one of the central hubs in the apoptosis regulatory network. This protein contains (from the N terminal) a caspase recruitment domain (CARD), an ATPase domain (NB-ARC), few short helical domains and then several copies of the WD40 repeat domain. Upon binding cytochrome c and dATP, this protein forms an oligomeric apoptosome. The apoptosome binds and cleaves Procaspase-9 protein, releasing its mature, activated form. The precise mechanism for this reaction is still debated though work published by Guy Salvesen suggests that the apoptosome may induce caspase-9 dimerization and subsequent autocatalysis. Activated caspase-9 stimulates the subsequent caspase cascade that commits the cell to apoptosis. Alternative splicing results in several transcript variants encoding different isoforms. APAF1 contains a CARD domain with a Greek key motif composed of six helices, a Rossman fold nucleotide binding domains, a short helical motif and a winged-helix domain. APAF1 has been shown to interact with: