Proteases compositions capable of binding to said site, and meth

Details Proteases compositions capable of binding to said site, and meth Proteases compositions capable of binding to said site, and meth

1997-05-09

2000-07-04

Wax, Robert A.

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving hydrolase

435 24, 435212, 435219, C12Q 137

Patent

active

06083711&

ABSTRACT:
Novel herpes viral protease crystalline structures are identified which have an active site formed by the three amino acids Ser, His and His. Also disclosed are methods of identifying inhibitors of these proteases and/or active sites.

REFERENCES:
Chen et al. "Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad" Cell 66, 835-843, Sep. 6, 1996.
Shieh et al. "Three-dimentional structure of human cytomegalovirus protease" Nature 383, 279-282, Sep. 19, 1996.
Hoog et al. "Active site cavity of herpesvirus protease revealed by crystal structure of herpes simplex virus protease/inhibitor complex" Biochemistry 36, 14023-14029, 1997.
Schmidt et al. "Dimerization and activation of the herpes simplex virus type 1 protease" J. Biol. Chem. 272, 7732-7735, Mar. 21, 1997.
Qui et al. "Unique fold and active site in cytomegalovirus" Nature 383, 275-279, Sep. 19, 1996.
Tong et al. "A new serine-protease fold revealed by crystal structure of human cytomegalovirus protease" Nature 383, 272-275, Sep. 19, 1996.
Qui et al. "Crystal structure of varicella-zoster virus protease" Proc. Natl. Acad. Sci. USA 94, 2874-2879, Apr. 1997.

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