Human E3 ubiquitin protein ligase

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving viable micro-organism

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4353201, 435325, 435375, 536 232, 536 245, C07H 2104, C12N 1500, C12N 500, C12Q 102

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active

060871229

ABSTRACT:
Human E3 ubiquitin protein ligase is described. A structural region which encodes the polypeptide is disclosed as well as the the amino acid residue sequence of the protein ligase. Methods are provided which employ the sequences to identify compounds that modulate a biological and/or pharmacological activity of the molecule and hence regulate cellular and tissue physiology. The invention is also drawn toward the diagnosis, prevention, and treatment of pathophysiological disorders mediated by E3 ubiquitin protein ligases.

REFERENCES:
Sigma Catalog, 1990, p 815 & 617.
Hochstrasser, Mark; Ubiquitin-Dependent Protein Degradation, Annu. Rev. Genet. 1996, 30:405-39.
Weissman, Alan M.; Regulating Protein Degradation by Ubiquitination, Review Immunology Today, vol. 18, No. 4 189, Apr. 1997.
Pahl, Heike L. et al.; Control of Gene Expression by Proteolysis, Current Opinion in Cell Biology 1996, 8:340-347.
Rolfe, Mark et al.; The Ubiquitin-Mediated Proteolytic Pathway as a Therapeutic Area, J. Mol. Med. (1997) 75:5-17.
Perry, William L. et al.; The Itchy Locus Encodes a Novel Ubiquitin Protein Ligase That is Disrupted in a .sup.18h Mice, Nature Genetics, vol. 18, Feb. 1998.
D'Andrea, Alan D., Relieving the Itch, Nature Genetics, vol. 18, Feb. 1998.
Wood, Jonathan D. et al.; Atrophin-1, the DRPLA Gene Product, Interacts with Two Families of WW Domain-Containing Proteins; Molecular and Cellular Neuroscience 11, 149-160 (1998), Article No. CN980677.

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