Cytotoxic ribonuclease variants

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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C530S402000, C424S185100

Reexamination Certificate

active

07655757

ABSTRACT:
This invention relates to cytotoxic variants of human ribonuclease 1 (RNase 1) identified through analysis of the interaction between RNase 1 and the human ribonuclease inhibitor (hRI) as defined by the three dimensional (3-D) atomic structure of the RNase 1 hRI complex. Also disclosed is the 3-D structure of the hRI.RNase 1 complex and methods for designing the RNase 1 variants.

REFERENCES:
patent: 5840296 (1998-11-01), Raines et al.
patent: 6280991 (2001-08-01), Raines
patent: 2005/0261232 (2005-11-01), Strong et al.
patent: WO0031242 (2000-03-01), None
patent: WO 00/40608 (2000-07-01), None
two sequence comparisons.
Gura (Science, 1997, 278:1041-1042.).
Pous et al (2000, J. Mol. Biol., 303:49-60).
Kobe and Delsenhofer (Mar. 9, 1995, Nature, 374(9):183-186).
Murthy and Sideshmukh (Biochem. J., 1992, 281: 343-348).
Burgess et al. (J. Cell. Biol. 111:2129-2138, 1990).
Lazar et al. (Mol. Cell Biol. 8:1247-1252, 1998).
Ontjes et al (PNAS, Oct. 1969, 64(2): 428-35).
Boix, E., et al., “Role of the N Terminus in RNase A Homologues: Differences in Catalytic Activity, Ribonuclease Inhibitor Interaction and Cytotoxicity,” J. Mol. Biol. 257:992-1007 (1996).
Bosch, M., et al., “A Nuclear Localization Sequence Endows Human Pancreatic Ribonuclease With Cytotoxic Activity,” Biochemistry 43:2167-2177 (2004).
Gaur, D., et al., “Interaction of Human Pancreatic Ribonuclease with Human Ribonuclease Inhibitor,” The Journal of Biological Chemistry 276:24978-24984 (2001).
Kobe, B., et al., “A structural basis of the interactions between leucine-rich repeats and protein ligands,” Nature 374:183-186 (1995).
Kobe, G., et al., “Mechanism of Ribonuclease Inhibition by Ribonuclease Inhibitor Protein Based on the crystal Structure of its Complex with Ribonuclease A,” J. Mol. Biol. 264:1028-1043(1996).
Kumar, K., et al., “Selective abolition of pancreatic RNase binding to its inhibitor protein,” PNAS 101:53-58 (2004).
Lee, J.E., et al., “Cytotoxicity of Bovine Seminal Ribonuclease: Monomer versus Dimer,” Biochemistry 44:15760-15767 (2005).
Leland, P.A., et al., “Ribonuclease A variants with potent cytotoxic activity,” Proc. Natl. Acad. Sci. USA 95:10407-10412 (1998).
Leland, P.A., et al., “Endowing Human Pancreatic Ribonuclease with Toxicity for Cancer Cells,” The Journal of Biological Chemistry 276:43095-43102 (2001).
Mitchell, J.C., et al., “Rapid atomic density methods for molecular shape characterization,” Journal of Molecular Graphics and Modelling 19:325-330 (2001).
Pous, J., et al., “Three-dimensional Structure of a Human Pancreatic Ribonuclease Variant, a Step Forward in the Design of Cytotoxic Ribonucleases,” J. Mol. Biol. 303:49-59 (2000).
Pous, J., et al., “Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution,” Acta Cryst. D57:498-505 (2001).
Rajamani, D., et al., “Archor residues in protein-protein interactions,” PNAS 101:11287-11292 (2004).
Rutkoski, T.J., et al., “Disruption of Shape-Complementarity Markers to Create Cytotoxic Variants of Ribonuclease A,” J. Mol. Biol. 354:41-54 (2005).
Shaul, Y., et al., “Exploring the Charge Space of Protein-Protein Association: A Proteomic Study,” Proteins: Structure, Function, and Bioinformatics 60:331-352 (2005).
Murphy, B.S., et al., “Sensitivity of monomeric and dimeric forms of bovine seminal ribonuclease to human placental ribonuclease inhibitor,” Biochem. J. 281:343-348 (1992).
Quintessence/Biosciences webpage on Evade TM Ribonucleases.

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