title: The finger domain of the human deubiquitinating enzyme HAUSP is a zinc ribbon.
abstract: Human deubiquitinating enzyme HAUSP is a cysteine protease that regulates the levels of the tumor suppressor protein p53. By comparative sequence and structural analysis, we show that the previously uncharacterized finger domain insert to the catalytic core of HAUSP is a zinc ribbon that has lost its zinc-binding ability.
authors.affiliation: Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9050, USA. krishna@chop.swmed.edu
authors.forename: S Sri
authors.initials: SS
authors.lastname: Krishna
authors.forename: Nick V
authors.initials: NV
authors.lastname: Grishin
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D010450:Endopeptidases / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D043222:Ubiquitin Thiolesterase; D000076084:Ubiquitin-Specific Peptidase 7; D016335:Zinc Fingers / Q000235:genetics
chemical_list: D010450:Endopeptidases; C464569:USP7 protein, human; D043222:Ubiquitin Thiolesterase; D000076084:Ubiquitin-Specific Peptidase 7