1a1z: Difference between revisions
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'''FADD DEATH EFFECTOR DOMAIN, F25G MUTANT, NMR MINIMIZED AVERAGE STRUCTURE''' | '''FADD DEATH EFFECTOR DOMAIN, F25G MUTANT, NMR MINIMIZED AVERAGE STRUCTURE''' | ||
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[[Category: Meadows, R P.]] | [[Category: Meadows, R P.]] | ||
[[Category: Ng, C.]] | [[Category: Ng, C.]] | ||
[[Category: | [[Category: Apoptosis]] | ||
[[Category: | [[Category: Death effector domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:41:21 2008'' | |||
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Revision as of 09:41, 2 May 2008
FADD DEATH EFFECTOR DOMAIN, F25G MUTANT, NMR MINIMIZED AVERAGE STRUCTURE
OverviewOverview
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 StructureAbout this Structure
1A1Z is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 09:41:21 2008