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1a1z

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a1z OCA], [http://www.ebi.ac.uk/pdbsum/1a1z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a1z RCSB]</span>
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[[Category: death effector domain]]
[[Category: death effector domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:20 2008''

Revision as of 15:31, 30 March 2008


PDB ID 1a1z

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



FADD DEATH EFFECTOR DOMAIN, F25G MUTANT, NMR MINIMIZED AVERAGE STRUCTURE


Overview

When activated, membrane-bound receptors for Fas and tumour-necrosis factor initiate programmed cell death by recruiting the death domain of the adaptor protein FADD to the membrane. FADD then activates caspase 8 (also known as FLICE or MACH) through an interaction between the death-effector domains of FADD and caspase 8. This ultimately leads to the apoptotic response. Death-effector domains and homologous protein modules known as caspase-recruitment domains have been found in several proteins and are important regulators of caspase (FLICE) activity and of apoptosis. Here we describe the solution structure of a soluble, biologically active mutant of the FADD death-effector domain. The structure consists of six antiparallel, amphipathic alpha-helices and resembles the overall fold of the death domains of Fas and p75. Despite this structural similarity, mutations that inhibit protein-protein interactions involving the Fas death domain have no effect when introduced into the FADD death-effector domain. Instead, a hydrophobic region of the FADD death-effector domain that is not present in the death domains is vital for binding to FLICE and for apoptotic activity.

About this Structure

1A1Z is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

NMR structure and mutagenesis of the FADD (Mort1) death-effector domain., Eberstadt M, Huang B, Chen Z, Meadows RP, Ng SC, Zheng L, Lenardo MJ, Fesik SW, Nature. 1998 Apr 30;392(6679):941-5. PMID:9582077

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