Otubain 2 (OTUB2) is a member of DUBs that belong to the ovarian tumour (OTU) superfamily of proteins which consists of a five-stranded beta-sheet sandwiched in between a small helical amino-terminal region consisting of alpha1 and alpha2, and a large helical region comprised of alpha3-alpha10. Like other DUBs, otubain 2 (OTUB2) cleaves proteins precisely at the ubiquitin-protein bond so that ubiquitylation process can be reversed and regulated. Otubain 2 (OTUB2)s active-site cleft is sterically occluded by a novel loop conformation resulting in an oxyanion hole, which consists uniquely of backbone amides. Furthermore, the residues that orient and stabilize the active-site histidine of otubain 2 (OTUB2) are different from other cysteine proteases. This reorganization of the active-site topology provides a possible explanation for the low turnover and substrate specificity of the otubains.
TMPY-02522
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