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| http://purl.uniprot.org/citations/9651369 | http://www.w3.org/2000/01/rdf-schema#comment | "The apoptotic machinery of Caenorhabditis elegans includes three core interacting components: CED-3, CED-4, and CED-9. CED-3 is a death protease composed of a prodomain and a protease domain. CED-4 is a P-loop-containing, nucleotide-binding molecule that complexes with the single polypeptide zymogen form of CED-3, promoting its activation by autoprocessing. CED-9 blocks death by complexing with CED-4 and suppressing its ability to promote CED-3 activation. A naturally occurring alternatively spliced form of CED-4 that contains an insertion within the nucleotide-binding region (CED-4L) functions as a dominant negative inhibitor of CED-3 processing and attenuates cell death. Domain mapping studies revealed that distinct regions within CED-4 bind to the CED-3 prodomain and protease domain. Importantly, the CED-4 P-loop was involved in prodomain binding. Disruption of P-loop geometry because of mutation of a critical lysine (K165R) or insertional inactivation (CED-4L) abolished prodomain binding. Regardless, K165R and CED-4L still retained CED-3 binding through the protease domain but were unable to initiate CED-3 processing. Therefore, the P-loop-prodomain interaction is critical for triggering CED-4-mediated CED-3 processing. Underscoring the importance of this interaction was the finding that CED-9 contacted the P-loop and selectively inhibited its interaction with the CED-3 prodomain. These results provide a simple mechanism for how CED-9 functions to block CED-4-mediated CED-3 processing and cell death."xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.28.17708"xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/author | "O'Rourke K."xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/author | "Dixit V.M."xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/author | "Chinnaiyan A.M."xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/author | "Chaudhary D."xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/pages | "17708-17712"xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/title | "The death inhibitory molecules CED-9 and CED-4L use a common mechanism to inhibit the CED-3 death protease."xsd:string |
| http://purl.uniprot.org/citations/9651369 | http://purl.uniprot.org/core/volume | "273"xsd:string |
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