Solution structure of RIP DD and uses thereof

Details Solution structure of RIP DD and uses thereof Solution structure of RIP DD and uses thereof

2008-05-27

2008-05-27

Clow, Lori A. (Department: 1631)

Data processing: measuring, calibrating, or testing

Measurement system in a specific environment

Biological or biochemical

C530S300000, C530S350000

Reexamination Certificate

active

10359439

ABSTRACT:
The present invention relates to the three dimensional solution structure of receptor interacting protein dead domain (RIP DD), as well as the identification and characterization of various binding active sites of RIP DD. Also provided for by the present invention are methods of utilizing the three dimensional structure for the design and selection of potent and selective inhibitors of TNF signaling pathways.

REFERENCES:
patent: 5674734 (1997-10-01), Leder et al.
patent: 6355780 (2002-03-01), Wallach et al.
patent: 2002/0094540 (2002-07-01), Tsao et al.
patent: 2002/0123117 (2002-09-01), Wallach et al.
patent: WO9625941 (1996-08-01), None
Arch et al., “Tumor necrosis factor receptor-associated factors (TRAFs)—a family of adapter proteins that regulates life and death,” Genes & Development, 12, 2821-2830, 1988.
Boldin et al., “Self-association of the “Death Domains” of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects,” The Journal of Biological Chemistry, 270 (1), 387-391, 1995.
Chou et al., “Solution Structure of the RAIDD CARD and Model for CARD/CARD Interaction in Caspase-2 and Caspase-9 Recruitment,” Cell, 94, 171-180, 1988.
Day et al., “Solution Structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1,” Cell Death and Differentiation, 6, 1125-1132, 1999.
Duan et al, “RAIDD is a new ‘death’ adaptor molecule,” Nature, 385, 86-89, Jan. 1997.
Eberstadt et al., “NMR structure and mutagenesis of the FADD (Mort1) death-effector domain,” Nature, 392, 941-945, 1998.
Eck et al., “Crystallization of Trimeric Recombinant Human Tumor Necrosis Factor (Cachectin),” The Journal of Biological Chemistry, 263 (26), 12816-12819,1988.
Feinstein et al., “The death domain: a module shared by proteins with diverse cellular functions,” Tibs, 20, 342-344, 1995.
Grell et al., “TR60 and TR80 Tumor Necrosis Factor (TNF)-Receptors Can Independently Mediate Cytolysis,” Lymphokine and Cytokine Research, 12, 143-148, 1992.
Hofmann et al., “The CARD domain: a new apoptotic signalling motif,” TIBS, 22, 155-156, 1997.
Hsu et al., “The TNF Receptor 1-Associated Protein TRADD Signals Cell Death and NF-κB Activation,” Cell, 81, 495-504, 1995.
Hsu et al, “TRADD—TRAF2 and TRADD-FADD Interactions Define Two Distinct TNF Receptor 1 Signal Transduction Pathways,” Cell, 84, 299-308, 1996.
Hsu et al, “TNF-Dependent Recruitment of the Protein Kinase RIP to the TNF Receptor-1 Signaling Complex,” Immunity, 4, 387-396, 1996.
Huang et al, “NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain,” Nature, 384, 638-641, 1996.
Jeong et al., “The Solution Structiure of FADD Death Domain,” The Journal of Biological Chemistry, 274(23), 16337-16342, 1999.
Kelliher et al., “The Death Domain Kinase RIP Mediates the TNF-Induced NF—κB Signal,” Immunity, 8, 297-303, 1998.
Kieser et al, “LMP1 signal transduction differs substantially from TNF receptor 1 signaling in the molecular functions of TRADD and TRAF2,” The EMBO Journal, 18(9), 2511-2521, 1999.
Liepinsh et al., “NMR structure of the death domain of the p75 neurotrophin receptor,” The EMBO Journal, 16 (16), 4999-5005, 1997.
McWhirter et al, “Crystallographic analysis of CD40 recognition and signaling by human TRAF2,” Proc. Natl. Acad. Sci. USA, 96, 8408-8413, 1999.
Nakano et al., “TRAF5, an Activator of NF-κB and Putative Signal Transducer for the Lymphotoxin-β Receptor,” The Journal of Biological Chemistry, 271 (25), 14661-14664, 1996.
Park et al., “Structural basis for self-association and receptor recognition of human TRAF2,” Nature, 398, 533-538, 1999.
Pullen et al., “CD40-Tumor Necrosis Factor Receptor-Associated Factor (TRAF) Interactions: Regulation of CD40 Signaling through Multiple TRAF Binding Sites and TRAF Hetero-Oligomerization,” Biochemistry, 37, 11836-11845, 1998.
Qin et al., “Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1,” Nature, 399, 549-557, 1999.
Sato et al., “A novel member of the TRAF family of putative signal transducing protein binds to the cytosolic domain of CD40,” FEBS Letters, 358, 113-118, 1995.
Sioud et al., “Design of Nuclease Resistant Protein Kinase CαDNA Enzymes with Potential Therapeutic Application,” J. Mol. Biol., 296, 937-947, 2000.
Stanger et al., “RIP: A Novel Protein Containing a Death Domain That Interacts with Fas/APO-1 (CD95) in Yeast and Causes Cell Death,” Cell, 81, 513-523, 1995.
Sukits et al., “Solution Structure of the Tumor Necrosis Factor Receptor-1 Death Domain,” J. Mol. Biol., 310, 895-906, 2001.
Tartaglia et al., “Tumor Necrosis Factor's Cytotoxic Activity Is Signaled by the p55 TNF Receptor,” Cell, 73, 213-216, 1993.
Telliez et al., “Mutational Analysis and NMR studies of the Death Domain of the Tumor Necrosis Factor Receptor-1,” J. Mol. Biol., 300, 1323-1333, 2000.
Vandevoorde et al., “Induced Expression of Trimerized Intracellular Domains of the Human Tumor Necrosis Factor (TNF) p55 Receptor Elicits TNF Effects,” The Journal of Cell Biology, 137 (7), 1627-1638, 1997.
Xiao et al., “Three-Dimensional Structure of a Complex between the Death Domains of Pelle and Tube,” Cell, 99, 545-555, 1999.
Zhou et al., “Solution Structure of Apaf-1 CARD and its interaction with caspase-9 CARD: A Structural basis for specific adaptor/caspase interaction,” Proc. Natl. Acad. Sci. USA, 96, 11265-11270, 1999.

Affiliated with

Also associated with

Rating

Solution structure of RIP DD and uses thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Solution structure of RIP DD and uses thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Solution structure of RIP DD and uses thereof will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3941144