1ddf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ddf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ddf OCA], [http://www.ebi.ac.uk/pdbsum/1ddf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ddf RCSB]</span>
}}
}}
Line 14: Line 17:
==Overview==
==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.
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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134637 134637]], Autoimmune lymphoproliferative syndrome, type IA OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134637 134637]], Squamous cell carcinoma, burn scar-related, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134637 134637]]
 
==About this Structure==
==About this Structure==
Line 36: Line 36:
[[Category: transmembrane]]
[[Category: transmembrane]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:36:40 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:26 2008''

Revision as of 16:39, 30 March 2008


PDB ID 1ddf

Drag the structure with the mouse to rotate
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE


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.

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

Page seeded by OCA on Sun Mar 30 19:39:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools