Abstract：
:Clip domains are structural modules found in arthropod serine proteinases and some proteolytically inactive homologues, which mediate extracellular signaling pathways of development and immunity. While little is known about their structures or functions, clip domains are proposed to be sites for interactions of proteinases with their activators, cofactors, and substrates. Here we report the solution structure of dual clip domains from Manduca sexta prophenoloxidase activating proteinase-2. Each domain adopts a new mixed alpha/beta fold (a three-stranded antiparallel beta-sheet flanked by two alpha-helices), and the architecture provides structural information on clip domains from a catalytically active proteinase for the first time. Examination of the structure in conjunction with a multiple sequence alignment of the clip domains from different groups suggests a substrate-binding site, a bacteria-interacting region, and a surface for specific interactions. In summary, our results provide insights into the structural basis of clip domain functions and this structure may represent the prototype of group-2 clip domains.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Huang R,Lu Z,Dai H,Velde DV,Prakash O,Jiang Hdoi
10.1021/bi7010724subject
Has Abstractpub_date
2007-10-16 00:00:00pages
11431-9issue
41eissn
0006-2960issn
1520-4995journal_volume
46pub_type
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