Related ArticlesNMR structure and mutagenesis of the FADD (Mort1) death-effector domain.
Nature. 1998 Apr 30;392(6679):941-5
Authors: Eberstadt M, Huang B, Chen Z, Meadows RP, Ng SC, Zheng L, Lenardo MJ, Fesik SW
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.
[NMR paper] Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis
Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and (19)F NMR spectroscopy.
Related Articles Oxygen as a paramagnetic probe of membrane protein structure by cysteine mutagenesis and (19)F NMR spectroscopy.
J Am Chem Soc. 2002 Feb 27;124(8):1778-81
Authors: Luchette PA, Prosser RS, Sanders CR
Oxygen solubility increases toward the hydrophobic interior of membranes. Using NMR, this O(2) solubility gradient gives rise to an exquisite range of position-dependent paramagnetic effects at partial pressures of 100...
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[NMR paper] NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis p
NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP.
Related Articles NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP.
J Biol Chem. 2000 Oct 27;275(43):33777-81
Authors: Sun C, Cai M, Meadows RP, Xu N, Gunasekera AH, Herrmann J, Wu JC, Fesik SW
The inhibitor of apoptosis proteins (IAPs) regulate the caspase family of cysteine proteases, which play an important role in the execution of programmed cell death. Human X-linked inhibitor of apoptosis...
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[NMR paper] Assignment of 1H, 13C and 15N NMR signals in the toluene 4-monooxygenase effector pro
Assignment of 1H, 13C and 15N NMR signals in the toluene 4-monooxygenase effector protein.
Related Articles Assignment of 1H, 13C and 15N NMR signals in the toluene 4-monooxygenase effector protein.
J Biomol NMR. 2000 Apr;16(4):359-60
Authors: Hemmi H, Studts JM, Chae YK, Markley JL, Fox BG
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[NMR paper] NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP.
NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP.
Related Articles NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP.
Nature. 1999 Oct 21;401(6755):818-22
Authors: Sun C, Cai M, Gunasekera AH, Meadows RP, Wang H, Chen J, Zhang H, Wu W, Xu N, Ng SC, Fesik SW
The inhibitor-of-apoptosis (IAP) family of proteins, originally identified in baculoviruses, regulate programmed cell death in a variety of organisms. IAPs inhibit specific enzymes (caspases) in the death cascade and contain one to three...
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[NMR paper] NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide
NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Related Articles NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor Trio.
Cell. 1998 Oct 16;95(2):269-77
Authors: Liu X, Wang H, Eberstadt M, Schnuchel A, Olejniczak ET, Meadows RP, Schkeryantz JM, Janowick DA, Harlan JE, Harris EA, Staunton DE, Fesik SW
Guanine nucleotide exchange factors for the Rho family of GTPases contain a Dbl homology (DH) domain responsible for catalysis and a...
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Solution NMR Investigation of the CD95/FADD Homotypic Death Domain Complex Suggests L
Solution NMR Investigation of the CD95/FADD Homotypic Death Domain Complex Suggests Lack of Engagement of the CD95 C Terminus.
Related Articles Solution NMR Investigation of the CD95/FADD Homotypic Death Domain Complex Suggests Lack of Engagement of the CD95 C Terminus.
Structure. 2010 Oct 13;18(10):1378-90
Authors: Esposito D, Sankar A, Morgner N, Robinson CV, Rittinger K, Driscoll PC
We have addressed complex formation between the death domain (DD) of the death receptor CD95 (Fas/APO-1) with the DD of immediate adaptor protein FADD using nuclear...
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[NMR paper] NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain.
NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain.
Nature. 1996 Dec 19-26;384(6610):638-41
Authors: Huang B, Eberstadt M, Olejniczak ET, Meadows RP, Fesik SW
Programmed cell death (apoptosis) mediated by the cytokine receptor Fas is critical for the removal of autoreactive T cells, the mechanism of immune privilege, and for maintenance of immune-system...
NMR structure and mutagenesis of the FADD (Mort1) death-effector domain.
Linear Mode
