2gf5
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(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 /> ...)
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Revision as of 20:11, 12 November 2007
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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
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