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USP7 Protein Crystal

(CBCRY35)  Download Datasheet
Background
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.
Molecular Description
Protein Classification
Hydrolase
Structure Weight
121067.00 Da
Polymer
1
Molecule
Ubiquitin carboxyl-terminal hydrolase 7
Chain Length
522 amino acids
Crystal Description
PDB ID
2F1Z
MMDB ID
37695
Source
E.coli
Method
X-Ray Diffraction
Resolution
3.2Å
Gene Information
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
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