Related ArticlesSolution 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 magnetic resonance (NMR) spectroscopy, mass spectrometry, and size-exclusion chromatography with in-line light scattering. We find complexation to be independent of the C-terminal 12 residues of CD95 and insensitive to mutation of residues that engage in the high-order clustering of CD95-DD molecules in a recently reported crystal structure obtained at pH 4. Differential NMR linewidths indicate that the C-terminal region of the CD95 chains remains in a disordered state and (13)C-methyl TROSY data are consistent with a lack of high degree of symmetry for the complex. The overall molecular mass of the complex is inconsistent with that in the crystal structure, and the complex dissociates at pH 4. We discuss these findings using sequence analysis of CD95 orthologs and the effect of FADD mutations on the interaction with CD95.
[NMR paper] An NMR investigation of solution aggregation reactions preceding the misassembly of a
An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils.
Related Articles An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils.
J Mol Biol. 1999 Sep 3;291(5):1191-206
Authors: Alexandrescu AT, Rathgeb-Szabo K
At pH 2.0, acid-denatured CspA undergoes a slow self-assembly process, which results in the formation of insoluble fibrils. 1H-15N HSQC, 3D HSQC-NOESY, and 15N T2 NMR experiments have...
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[NMR paper] The NMR structure of the RNA binding domain of E. coli rho factor suggests possible R
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Related Articles The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Nat Struct Biol. 1998 May;5(5):393-9
Authors: Briercheck DM, Wood TC, Allison TJ, Richardson JP, Rule GS
Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding...
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[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...
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[NMR paper] Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin
Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR.
Biochemistry. 1997 Sep 30;36(39):11605-18
Authors: Bentrop D, Bertini I, Cremonini MA, Forsén S, Luchinat C, Malmendal A
The solution structure of the dicerium(III) complex of the N-terminal domain of calmodulin...
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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...
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[NMR paper] Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular d
Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data.
Related Articles Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data.
Protein Eng. 1995 Nov;8(11):1117-28
Authors: Li A, Daggett V
The native solution structure and dynamics of chymotrypsin inhibitor 2 (CI2) have been studied using a long (5.3 ns) molecular dynamics (MD) simulation without any imposed...
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[NMR paper] 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repr
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
Related Articles 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
J Biomol Struct Dyn. 1991 Dec;9(3):447-61
Authors: Ottleben G, Messori L, Rüterjans H, Kaptein R, Granger-Schnarr M, Schnarr M
A synthetic half-operator DNA-duplex, d(GCTACTGTATGT), containing a portion of the proposed recognition sequence (CTGT) of several "SOS" genes, has been...
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[NMR paper] 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repr
1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
Related Articles 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator.
J Biomol Struct Dyn. 1991 Dec;9(3):447-61
Authors: Ottleben G, Messori L, Rüterjans H, Kaptein R, Granger-Schnarr M, Schnarr M
A synthetic half-operator DNA-duplex, d(GCTACTGTATGT), containing a portion of the proposed recognition sequence (CTGT) of several "SOS" genes, has been...