Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases

The Journal of Biological Chemistry
Cynthia TallantF Xavier Gomis-Rüth

Abstract

The metzincin clan encompasses several families of zinc-dependent metalloproteases with proven function both in physiology and pathology. They act either as broad spectrum protein degraders or as sheddases, operating through limited proteolysis. Among the structurally uncharacterized metzincin families are the pappalysins, of which the most thoroughly studied member is human pregnancy-associated plasma protein A (PAPP-A), a heavily glycosylated 170-kDa multidomain protein specifically cleaving insulin-like growth factor (IGF)-binding proteins (IGFBPs). Proulilysin is a 38-kDa archaeal protein that shares sequence similarity with PAPP-A but encompasses only the pro-domain and the catalytic domain. It undergoes calcium-mediated autolytic activation, and the mature protein adopts a three-dimensional structure with two subdomains separated by an active site cleft containing the catalytic zinc ion. This structure is reminiscent of human members of the adamalysin/ADAMs (a disintegrin and a metalloprotease) family of metzincins. A bound dipeptide yields information on the substrate specificity of ulilysin, which specifically hydrolyzes IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Accordingly, ul...Continue Reading

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Citations

Sep 23, 2009·Dalton Transactions : an International Journal of Inorganic Chemistry·Sérgio Filipe SousaMaria João Ramos
Mar 6, 2010·The Journal of Biological Chemistry·Cynthia TallantF Xavier Gomis-Rüth
Mar 6, 2010·The Journal of Biological Chemistry·Tibisay GuevaraF Xavier Gomis-Rüth
Feb 10, 2009·The Journal of Biological Chemistry·F Xavier Gomis-Rüth
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