The Fas receptor is a representative death receptor, and the Fas-associated protein with death domain (FADD) is a crucial adapter protein needed to support the Fas receptor's activity. The Fas-FADD interactions constitute an important signaling pathway that ultimately induces apoptosis or programmed cell death in biological systems. The interactions responsible for this cell-death process are governed by the binding process of the Fas ligand to the Fas, followed by the caspase cascade activation. Using a computational approach, the present communication explores certain essential structural aspects of the Fas-FADD death domains and their interfacial interactions.
The Fas receptor is a representative death receptor, and the Fas-associated protein with death domain (FADD) is a crucial adapter protein needed to support the Fas receptor's activity. The Fas-FADD interactions constitute an important signaling pathway that ultimately induces apoptosis or programmed cell death in biological systems. The interactions responsible for this cell-death process are governed by the binding process of the Fas ligand to the Fas, followed by the caspase cascade activation. Using a computational approach, the present communication explores certain essential structural aspects of the Fas-FADD death domains and their interfacial interactions.The Fas receptor is a representative death receptor, and the Fas-associated protein with death domain (FADD) is a crucial adapter protein needed to support the Fas receptor's activity. The Fas-FADD interactions constitute an important signaling pathway that ultimately induces apoptosis or programmed cell death in biological systems. The interactions responsible for this cell-death process are governed by the binding process of the Fas ligand to the Fas, followed by the caspase cascade activation. Using a computational approach, the present communication explores certain essential structural aspects of the Fas-FADD death domains and their interfacial interactions.
References:
1.Strasser A, et al. Immunity. 2009;30(2):180–192.
Cat. No. | Product Name | CAS No. | Information |
---|---|---|---|
H1628 |
SLV peptide |
189109-89-5 | A tripeptide representing the Fas-C terminus that specifically blocks the interaction of Fap1 with Fas; increases apoptosis sensitivity and decreases β-catenin in vitro, also decrease interaction of Fap1 with Apc, does not alter expression of Fap1 or Apc proteins; induces Fas-mediated apoptosis in a colon cancer cell line that expresses both Fas and FAP-1. |
H1627 |
Quinobene |
140942-13-8 | A HIV-1 surface-membrane inhibitor, also is a Fap1-blocking small molecule that replicates SLV peptied functions; blocks co-immunoprecipitation of Fas or Apc with Fap1, decreases β-catenin and survivin in Bcr-abl+ murine bone marrow cells; does not alter Fap1-independent Bcr-abl targets, impairs Bcr-abl+ cell outgrowth. |
H1626 |
KR-33494 |
1021497-97-1 | A potent inhibitor for Fas-mediated cell death, FAF1, inhibits ischemic cell death. |
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