[HTML][HTML] The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors
PE Van den Steen, I Van Aelst, V Hvidberg… - Journal of Biological …, 2006 - ASBMB
Gelatinase B/matrix metalloproteinase-9 (MMP-9), a key regulator and effector of immunity,
contains a C-terminal hemopexin domain preceded by a unique linker sequence of∼ 64
amino acid residues. This linker sequence is demonstrated to be an extensively O-
glycosylated (OG) domain with a compact three-dimensional structure. The OG and
hemopexin domains have no influence on the cleavage efficiency of MMP-9 substrates. In
contrast, the hemopexin domain contains a binding site for the cargo receptor low density …
contains a C-terminal hemopexin domain preceded by a unique linker sequence of∼ 64
amino acid residues. This linker sequence is demonstrated to be an extensively O-
glycosylated (OG) domain with a compact three-dimensional structure. The OG and
hemopexin domains have no influence on the cleavage efficiency of MMP-9 substrates. In
contrast, the hemopexin domain contains a binding site for the cargo receptor low density …