The finger domain of the human deubiquitinating enzyme HAUSP is a zinc ribbon.
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.
Krishna
S Sri
SS
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9050, USA. krishna@chop.swmed.edu
Grishin
Nick V
NV
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
D010450:Endopeptidases; C464569:USP7 protein, human; D043222:Ubiquitin Thiolesterase; D000076084:Ubiquitin-Specific Peptidase 7