Protein logic gates

Details Protein logic gates Protein logic gates

2003-07-03

2009-10-20

Clow, Lori A (Department: 1631)

Drug, bio-affecting and body treating compositions

Antigen, epitope, or other immunospecific immunoeffector

Fusion protein or fusion polypeptide

Reexamination Certificate

active

07604805

ABSTRACT:
Protein logic gates are made from autoregulated fusion proteins comprising an output domain and a plurality of input domains, wherein at least one of the input domains is heterologous to the output domain, and the input domains interact with each other to allosterically and external, ligand-dependently regulate the output domain. The output domain may be constitutively active, and in the absence of the ligand, the input domains interact to inhibit the output domain. The activity of the output domain is user discretionary, and may include activities that are catalytic, label-generative, metabolic-regulative, apototic, specific-binding, etc. Multiple input domains can cooperatively regulate the fusion protein in a wide variety of functionalities, including as an OR-gate, an AND-gate, and an AND-NOT-gate. The gates may be incorporated into cells and therein used to modulate cell function.

REFERENCES:
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Kim, “Expression and purificaion of recombinant immunotoxin-a fusion protein stabilizes a single-chain Fv (scFv) in denaturing condition,” Protein Expression and Purification, vol. 27 (2003), pp. 85-89.
Baker et al. “Protein Structure Prediction and Structural Genomics,” Science, vol. 294 (2001) pp. 93-96.
Seffernick et al. “Melamine Deaminase and Atrazine Chlorohydralase: 98 percent identical but functionally different,” Journal of Bacteriology, vol. 183 (2001) p. 2405-2410.
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Pedalacq et al., “Engineering soluble proteins for structural genomics,” vol. 20 (2002) pp. 927-932.
Dueber et al., “Reprogramming Control of an Allosteric Signaling Switch Through Modular Recombination,” Science, 2003 vol. 301, pp. 1904-1908.

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