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Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease
FEBS Letters
|October 8, 1998
Abstract:
Glycosaminoglycan attachment to perlecan domain I (173 residues) was completely prevented by site-directed mutagenesis of Ser-65, Ser-71 and Ser-76 as shown by recombinant production in mammalian cells. This did not interfere with the proper folding of the domain's SEA module but enhanced its sensitivity to neutral proteases. Lack of substitution also abolished binding to the two major heparin binding sites of laminin-1.