1ddf
From Proteopedia
(New page: 200px<br /> <applet load="1ddf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ddf" /> '''FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE ST...) |
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'''FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Programmed cell death (apoptosis) mediated by the cytokine receptor Fas is | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1DDF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fesik, S.]] | [[Category: Fesik, S.]] | ||
[[Category: Huang, B.]] | [[Category: Huang, B.]] | ||
| - | [[Category: Meadows, R | + | [[Category: Meadows, R P.]] |
[[Category: Olejniczak, E.]] | [[Category: Olejniczak, E.]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:30 2008'' |
Revision as of 10:15, 21 February 2008
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FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Autoimmune lymphoproliferative syndrome OMIM:[134637], Autoimmune lymphoproliferative syndrome, type IA OMIM:[134637], Squamous cell carcinoma, burn scar-related, somatic OMIM:[134637]
About this Structure
1DDF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain., Huang B, Eberstadt M, Olejniczak ET, Meadows RP, Fesik SW, Nature. 1996 Dec 19-26;384(6610):638-41. PMID:8967952
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