Retrovirus protease characterized as a dimeric aspartic proteinase
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چکیده
منابع مشابه
Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease.
Recombinant human immunodeficiency virus 1 (HIV-1) protease, purified from a bacterial expression system, processed a recombinant form of its natural substrate, Pr55gag, into protein fragments that possess molecular weights commensurate with those of the virion gag proteins. Molecular weights of the protease obtained under denaturing and nondenaturing conditions (11,000 and 22,000, respectively...
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The structure of Rous sarcoma virus protease has been solved by multiple isomorphous replacement in the crystal form belonging to space group P3(1)21, with unit-cell parameters a = 88.95 A and c = 78.90 A. The enzyme belongs to the family of aspartic proteases with two identical subunits composing the active homodimer. The noncrystallographic dyad relating these two subunits was identified afte...
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Aspartic proteases are a relatively small group of enzymes which express in various nematodes including Onchocerca volvulus. An estimation of the gene copy number corresponding to the OV7A clone, which contains a cDNA insert encoding approximately two-thirds of the entire coding sequence of aspartic protease of O. volvulus, was made by slot blot analysis in a closely related species O. gibsonig...
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Aspartic proteases are relatively a small group of proteolytic enzymes. Over the last decade, they have received tremendous research interest as potential targets for pharmaceutical intervention as many have been shown to play significant roles in physiological and pathological processes. Despite numerous efforts, however, the only inhibitors for aspartic proteases currently in the market are d...
متن کاملSecreted aspartic proteinase family of Candida tropicalis.
Medically important yeasts of the genus Candida secrete aspartic proteinases (Saps), which are of particular interest as virulence factors. Like Candida albicans, Candida tropicalis secretes in vitro one dominant Sap (Sapt1p) in a medium containing bovine serum albumin (BSA) as the sole source of nitrogen. Using the gene SAPT1 as a probe and under low-stringency hybridization conditions, three ...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1989
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.63.5.2226-2232.1989