Ancillary domains, some of which are involved in substrate recognition, are also depicted.
This review will highlight these recent structures, particularly the non-catalytic ancillary domains, which might be important for substrate recognition.
The present review will highlight these structures, particularly the non-catalytic ancillary domains of P-III SVMPs and ADAMs that may target the enzymes to specific substrates.
However, a common theme is that a single conserved domain (often the nucleoside triphosphate binding domain) is combined with ancillary domains that provide the variation in substrate binding and function.
This superfamily contains secreted ADAMTS metalloproteases as well as ADAMTS-like proteins, which are not proteases, but secreted glycoproteins whose domain structure resembles the C-terminal ancillary domains of ADAMTS proteases [26].
ADAMTS-5 is a multi-domain metalloproteinase and its ancillary domains are essential for aggrecanolytic activity [ 3]; therefore, both the Cat and the ancillary domains are potential targets for inhibitory antibody development.
This suggests that the ancillary domains in the prokaryotic trypsin homologues may contribute to diversification in their function.
Studies of ADAMTS-4 have given an insight into the influence of the ancillary domains on the proteinase activities.
These data suggest that the catalytic activity of the USP11 protease domain is not modulated through ancillary domains using ubiquitin-AMC as model substrate.
Other common examples of ancillary domains seen in WDR proteins from yeast, animals or plants include the F-box, SET domain, and bromodomain (not shown).
