Related ArticlesNMR 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 homeostasis. Signalling of programmed cell death involves the self-association of a conserved cytoplasmic region of Fas called the death domain and interaction with another death-domain-containing protein, FADD (also known as MORT1). Although death domains are found in several proteins, their three-dimensional structure and the manner in which they interact is unknown. Here we describe the solution structure of the Fas death domain, as determined by NMR spectroscopy. The structure consists of six antiparallel, amphipathic alpha-helices arranged in a novel fold. From the structure and from site-directed mutagenesis, we have identified the region of the death domain involved in self-association and binding to the downstream signalling partner FADD.
[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...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[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...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[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...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[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...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] NMR structure and mutagenesis of the FADD (Mort1) death-effector domain.
NMR structure and mutagenesis of the FADD (Mort1) death-effector domain.
Related Articles NMR 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...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
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...
nmrlearner
Journal club
0
10-16-2010 03:56 PM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
J Biomol NMR. 2010 Aug;47(4):283-8
Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain.
Linear Mode
