USP7 Protein Crystal

Background

Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7), a deubiquitylating enzyme of the ubiquitin-specific processing protease family, specifically deubiquitylates both p53 and MDM2, hence playing an important yet enigmatic role in the p53-MDM2 pathway.

Protein Classification

Hydrolase

Structure Weight

121067.00 Da

Polymer

1

Molecule

Ubiquitin carboxyl-terminal hydrolase 7

Chain Length

522 amino acids

PDB ID

2F1Z

MMDB ID

37695

Source

E.coli

Method

X-Ray Diffraction

Resolution

3.2Å

Gene Name

USP7

Synonyms

HAUSP; TEF1; EC 3.1.2.15; Herpes virus-associated ubiquitin-specific protease; ubiquitin specific peptidase 7; ubiquitin specific protease 7 (herpes virus-associated); deubiquitinating enzyme 7; Ubiquitin thioesterase 7

UniProt ID

Q93009

Gene ID

7874

Chromosome Location

16p13.3

Function

cysteine-type endopeptidase activity; ubiquitin thiolesterase activity; protein binding; protein C-terminus binding; peptidase activity; cysteine-type peptidase activity; hydrolase activity

Reference

Hu, M., Gu, L., Li, M., Jeffrey, P.D., Gu, W., Shi, Y. (2006) Structural Basis of Competitive Recognition of p53 and MDM2 by HAUSP/USP7: Implications for the Regulation of the p53-MDM2 Pathway. Plos Biol. 4: e27-e27