Structural variability of the ubiquitin specific protease DUSP-UBL double domains

• DOI: 10.1016/j.febslet.2011.09.040
• Publication Date: 2011-10-16T19:30:29Z
• Authors: Paul R. Elliott; Han Liu; Martyna W. Pastok; Günter J. Grossmann; Daniel J. Rigden; Michael J. Clague; Sylvie Urbé; Igor L. Barsukov
• Keywords: Models, Molecular; 0301 basic medicine; DUSP; Molecular Sequence Data; Ubiquitin specific protease; Crystallography, X-Ray; Protein Structure, Tertiary; X-ray; 03 medical and health sciences; UBL; Endopeptidases; Humans; Amino Acid Sequence; Thiolester Hydrolases; Ubiquitin-Specific Proteases; Protein Multimerization; Protein Structure, Quaternary; Ubiquitin Thiolesterase

USP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP) family of deubiquitinating enzymes. The DUSP domain and the UBL domain in these proteins are juxtaposed which may provide a functional unit conferring specificity. We determined the structures of the USP15 DUSP-UBL double domain unit in monomeric and dimeric states. We then conducted comparative analysis of the structural and physical properties of all three DUSP-UBL units. We identified structural features that dictate different dispositions between constituent domains, which in turn may influence respective binding properties.