2gf5
From Proteopedia
(New page: 200px<br /> <applet load="2gf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gf5" /> '''Structure of intact FADD (MORT1)'''<br /> ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2gf5.gif|left|200px]]<br /> | + | [[Image:2gf5.gif|left|200px]]<br /><applet load="2gf5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2gf5" size=" | + | |
caption="2gf5" /> | caption="2gf5" /> | ||
'''Structure of intact FADD (MORT1)'''<br /> | '''Structure of intact FADD (MORT1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of FADD has been solved in solution, revealing that the | + | The structure of FADD has been solved in solution, revealing that the death effector domain (DED) and death domain (DD) are aligned with one another in an orthogonal, tail-to-tail fashion. Mutagenesis of FADD and functional reconstitution with its binding partners define the interaction with the intracellular domain of CD95 and the prodomain of procaspase-8 and reveal a self-association surface necessary to form a productive complex with an activated "death receptor." The identification of a procaspase-specific binding surface on the FADD DED suggests a preferential interaction with one, but not both, of the DEDs of procaspase-8 in a perpendicular arrangement. FADD self-association is mediated by a "hydrophobic patch" in the vicinity of F25 in the DED. The structure of FADD and its functional characterization, therefore, illustrate the architecture of key components in the death-inducing signaling complex. |
==About this Structure== | ==About this Structure== | ||
| - | 2GF5 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:// | + | 2GF5 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=2GF5 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carrington, P | + | [[Category: Carrington, P E.]] |
[[Category: Gavathiotis, E.]] | [[Category: Gavathiotis, E.]] | ||
| - | [[Category: Hill, J | + | [[Category: Hill, J M.]] |
[[Category: Huang, T.]] | [[Category: Huang, T.]] | ||
[[Category: Morisawa, G.]] | [[Category: Morisawa, G.]] | ||
[[Category: Sandu, C.]] | [[Category: Sandu, C.]] | ||
[[Category: Wei, Y.]] | [[Category: Wei, Y.]] | ||
| - | [[Category: Werner, M | + | [[Category: Werner, M H.]] |
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: death domain]] | [[Category: death domain]] | ||
| Line 27: | Line 26: | ||
[[Category: death-inducing signaling complex]] | [[Category: death-inducing signaling complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:04 2008'' |
Revision as of 15:31, 21 February 2008
|
Structure of intact FADD (MORT1)
Overview
The structure of FADD has been solved in solution, revealing that the death effector domain (DED) and death domain (DD) are aligned with one another in an orthogonal, tail-to-tail fashion. Mutagenesis of FADD and functional reconstitution with its binding partners define the interaction with the intracellular domain of CD95 and the prodomain of procaspase-8 and reveal a self-association surface necessary to form a productive complex with an activated "death receptor." The identification of a procaspase-specific binding surface on the FADD DED suggests a preferential interaction with one, but not both, of the DEDs of procaspase-8 in a perpendicular arrangement. FADD self-association is mediated by a "hydrophobic patch" in the vicinity of F25 in the DED. The structure of FADD and its functional characterization, therefore, illustrate the architecture of key components in the death-inducing signaling complex.
About this Structure
2GF5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of FADD and its mode of interaction with procaspase-8., Carrington PE, Sandu C, Wei Y, Hill JM, Morisawa G, Huang T, Gavathiotis E, Wei Y, Werner MH, Mol Cell. 2006 Jun 9;22(5):599-610. PMID:16762833
Page seeded by OCA on Thu Feb 21 17:31:04 2008
