2gf5: Difference between revisions

[[Image:2gf5.gif|left|200px]]<br /><applet load="2gf5" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

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].  

[[Category: Carrington, P E.]]

[[Category: Hill, J M.]]

[[Category: Werner, M H.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:04 2008''