2GF5

Structure of intact FADD (MORT1)

Summary for 2GF5

• Entry DOI: 10.2210/pdb2gf5/pdb
• Descriptor: FADD protein (1 entity in total)
• Functional Keywords: death domain, death effector domain, apoptosis, death-inducing signaling complex
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 21541.43

Authors

Carrington, P.E.,Sandu, C.,Wei, Y.,Hill, J.M.,Morisawa, G.,Huang, T.,Gavathiotis, E.,Wei, Y.,Werner, M.H. (deposition date: 2006-03-21, release date: 2006-06-27, Last modification date: 2024-05-29)

Primary citation

Carrington, P.E.,Sandu, C.,Wei, Y.,Hill, J.M.,Morisawa, G.,Huang, T.,Gavathiotis, E.,Wei, Y.,Werner, M.H.
The Structure of FADD and Its Mode of Interaction with Procaspase-8
Mol.Cell, 22:599-610, 2006

PubMed Abstract: 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.

PubMed: 16762833
DOI: 10.1016/j.molcel.2006.04.018

Experimental method

SOLUTION NMR