1a1w
From Proteopedia
(New page: 200px<br /> <applet load="1a1w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a1w" /> '''FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NM...) |
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'''FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE'''<br /> | '''FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A1W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1A1W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: death effector domain]] | [[Category: death effector domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:28:06 2008'' |
Revision as of 13:28, 15 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
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