Engineered protein kinases which can utilize nucleotide...

Details Engineered protein kinases which can utilize nucleotide... Engineered protein kinases which can utilize nucleotide...

2006-04-11

2006-04-11

Wilson, James O. (Department: 1623)

Organic compounds -- part of the class 532-570 series

Organic compounds

Carbohydrates or derivatives

C536S023200, C536S023600, C536S023700, C536S024310, C536S024500, C536S024320, C536S024330, C514S013800, C514S014800, C514S228200, C514S04400A, C435S006120, C435S069100, C435S015000, C435S193000, C424S193100

Reexamination Certificate

active

07026461

ABSTRACT:
Engineered protein kinases which can utilize modified nucleotide triphosphate substrates that are not as readily utilized by the wild-type forms of those enzymes, and methods of making and using them. Modified nucleotide triphosphate substrates and methods of making and using them. Methods for using such engineered kinases and such modified substrates to identify which protein substrates the kinases act upon, to measure the extent of such action, and to determine if test compounds can modulate such action. Also Engineered forms of multi-substrate enzymes which covalently attach part or all of at least one (donor) substrate to at least one other (recipient) substrate, which engineered forms will accept modified substrates that are not as readily utilized by the wild-type forms of those enzymes. Methods for making and using such engineered enzymes. Modified substrates and methods of making and using them. Methods for using such engineered enzymes and such modified substrates to identify the recipient substrates the enzymes act upon, to measure the extent of such action, and to measure whether test compounds modulate such action.

REFERENCES:
patent: 5620676 (1997-04-01), Jacobson et al.
patent: 6019966 (2000-02-01), Coleman et al.
patent: 6162613 (2000-12-01), Su et al.
patent: 6521417 (2003-02-01), Shokat
patent: WO 99/42592 (1999-08-01), None
Belshaw et al., Rational design of orthogonal receptor-ligand combinations, Angw. Chem. Int. Ed. Engl. 34:2129-2132 (1995).
Bishop et al., Design of allele-specific inhibitors to probe protein kinase signalling. Curr. Biol. 8:257-266 (1998).
Bishop et al., Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genetic approach, J. Am. Chem. Soc. 121:627-631 (1999).
Bishop et al., Acquisition of inhibitor-sensitive protein kinases through protein design, Pharmacol. Therapeut. 82:337-346 (1999).
Bishop et al., A chemical switch for inhibitor-sensitive alleles of any protein kinase. Nature 407:395-401 (2000).
Bolen et al., The Src family of tyrosine protein kinases in hemopoietic signal transduction, FASEB J. 6:3403-3409 (1992).
Brown et al., Regulation, substrantes and functions of Src, Biochemica et Biophysica Acta 1287:121-149 (1996).
Brugge et al., Identification of a transformation-specific antigen induced by an avian sarcoma virus, Nature 269:346-348 (1977).
Cicchetti et al., Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho, Science 257:803-806 (1992).
Cohen et al., Modular binding domains in signal transduction proteins. Cell 80:237-248 (1995).
Eck et al., Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck, Nature 362:87-91 (1993).
Eiseman, Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature 355:78-80 (1992).
Erpel et al., Src family protein tyrosine kinases and cellular signal transduction pathways, Curr. Opin. Cell Biol. 7:176-182 (1995).
Faltynek et al., Damnacanthal is a highly potent, selective inhibitor of p56lcktyrosine kinase activity, Biochem. 434:12404-12410 (1995).
Hanke et al., Discovery of a novel, potent Src-family selective tyrosine inhibitor, J. Biol. Chem. 271:695-701 (1996).
Hanks et al., Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members, Methods in Enzymology, 200:38-81 (1991).
Hunter, A thousand and one protein kinases. Cell 50:823-829 (1987).
Hunter, Protein kinases and phosphates: the yin and yang of protein phosphorylation and signaling. Cell 80:225-236 (1995).
Hwang et al., A Mutation that Alters the Nucleotide Specificity of Elongation Factor Tu, a GTP Regulatory Protein, J. Biol. Chem. 262:13081-13085 (1987).
Jove et al., Cell transformation by the viral src oncogene. Ann.Rev. Cell. Biol. 3:31-56 (1987).
Kamps et al., Most of the substrates of oncogenic viral tyrosine protein kinases can be phosphorylated by cellular tyrosine protein kinases in normal cells. Oncogene Res. 3:105-115 (1988).
Kipreos et al., Cell cycle-regulated binding of c-abl tyrosine kinase to DNA, Science 256:382-385 (1992).
Koyama et al., Structure of the Pl3k Sh3 domain and analysis of the SH3 Family, Cell 72:945-952 (1993).
Liu et al., A molecular gate which controls unnatural ATP analogue recognition by the tyrosine kinase v-Src, Bioorganic Med. Chem. 6:1219-1226 (1998).
Mayer et al., Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo, Mol. Cell. Biol. 12:609-618 (1992).
Mayer et al., Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the abl tyrosine kinase, Mol. Cell. Biol. 14:2883-2894 (1994).
Mustelin, T Cell antigen receptor signaling: three families of tyrosine kinases and a phosphatase, Immunity 1:351-356 (1994).
Pawson, Protein modules and signalling networks. Nature 373:573-580 (1995).
Renshaw et al:, Oncogenic v-Abl tyrosine kinase can inhibit or stimulate growth, depending on the cell context, EMBO J. 11:3941-3951 (1992).
Sawyers et al., The nuclear tyrosine kinase c-Abl negatively regulates cell growth, Cell 77:121-131 (1994).
Shaw et al., Engineering unatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates, Proc. Natl. Acad. Sci. USA 94:3565-3570 (1997).
Songyang et al., Catalytic specificity of protein-tyrosine kinases is critical for selective signalling, Nature 373:536-539 (1995).
Taylor et al., The cell cycle and c-Src, Curr. Opin. Genet. Dev. 3:26-34 (1993).
Ullrich et al., Signal transduction by receptors with tyrosine kinase activity, Cell 61:203-212 (1990).
Velazquez et al., A protein tyrosine kinase in the interferon alpha/beta signaling pathway, Cell 70:313-320 (1992).
Waksman et al., Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides, Nature 358:646-653 (1992).
Waksman et al., Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms, Cell 72:779-790 (1993).
Weijland et al., Toward a Model for the Interaction Between Elongation Factor Tu and the Ribosome, Science 259:1311-1314 (1993).
Vu et al., Solution Structure of the SH3 domain of Src and identification of its ligand-binding site, Science 258:1665-1668 (1992).
International Preliminary Examination Report from PCT/US00/02522 (dated May 19, 1999).
International Search Report from PCT/US00/02522 (dated Oct. 22, 1998).

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