1a1w
From Proteopedia
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==Overview== | ==Overview== | ||
| - | When activated, membrane-bound receptors for Fas and tumour-necrosis | + | 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== | ==About this Structure== | ||
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[[Category: Chen, Z.]] | [[Category: Chen, Z.]] | ||
[[Category: Eberstadt, M.]] | [[Category: Eberstadt, M.]] | ||
| - | [[Category: Fesik, S | + | [[Category: Fesik, S W.]] |
[[Category: Huang, B.]] | [[Category: Huang, B.]] | ||
| - | [[Category: Meadows, R | + | [[Category: Meadows, R P.]] |
[[Category: Ng, C.]] | [[Category: Ng, C.]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: death effector domain]] | [[Category: death effector domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:54 2008'' |
Revision as of 09:39, 21 February 2008
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FADD DEATH EFFECTOR DOMAIN, F25Y 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
1A1W 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
Page seeded by OCA on Thu Feb 21 11:39:54 2008
