1a1w
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1a1w.jpg|left|200px]] | + | [[Image:1a1w.jpg|left|200px]] |
| - | + | ||
| - | '''FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE''' | + | {{Structure |
| + | |PDB= 1a1w |SIZE=350|CAPTION= <scene name='initialview01'>1a1w</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1A1W is a [ | + | 1A1W is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9582077 9582077] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: death effector domain]] | [[Category: death effector domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:44 2008'' |
Revision as of 07:51, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 09:51:44 2008
