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NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain.
- Source :
-
Nature [Nature] 1996 Dec 19-26; Vol. 384 (6610), pp. 638-41. - Publication Year :
- 1996
-
Abstract
- Programmed cell death (apoptosis) mediated by the cytokine receptor Fas is critical for the removal of autoreactive T cells, the mechanism of immune privilege, and for maintenance of immune-system homeostasis. Signalling of programmed cell death involves the self-association of a conserved cytoplasmic region of Fas called the death domain and interaction with another death-domain-containing protein, FADD (also known as MORT1). Although death domains are found in several proteins, their three-dimensional structure and the manner in which they interact is unknown. Here we describe the solution structure of the Fas death domain, as determined by NMR spectroscopy. The structure consists of six antiparallel, amphipathic alpha-helices arranged in a novel fold. From the structure and from site-directed mutagenesis, we have identified the region of the death domain involved in self-association and binding to the downstream signalling partner FADD.
- Subjects :
- Amino Acid Sequence
Antigens, CD chemistry
Binding Sites
Escherichia coli
Humans
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Binding
Receptors, Tumor Necrosis Factor chemistry
Receptors, Tumor Necrosis Factor, Type I
Recombinant Proteins chemistry
Recombinant Proteins genetics
Sequence Homology, Amino Acid
Protein Conformation
fas Receptor chemistry
fas Receptor genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 384
- Issue :
- 6610
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 8967952
- Full Text :
- https://doi.org/10.1038/384638a0