Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
Yang, V. W-C, LaBrenz, S., Rosenberg, L., McQuillan, D., and Hook, M.
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------>vol=274
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------>journal_name=J. Biol. Chem.
------>paper_name=Decorin is a Zn2+ Metalloprotein
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------>fullAbstract=Decorin is ubiquitously distributed in the extracellular matrix of mammals and a member of the proteoglycan family characterized by a core protein dominated by leucine-rich repeat motifs. We show here that decorin extracted from bovine tissues under denaturing conditions or produced in recombinant "native" form by cultured mammalian cells has a high affinity for Zn2+ as demonstrated by equilibrium dialyses. The Zn2+-binding sites are localized to the N-terminal domain of the core protein that contains 4 Cys residues in a spacing reminiscent of a zinc finger. A recombinant 41-amino acid long peptide representing the N-terminal domain of decorin has full Zn2+ binding activity and binds two Zn2+ ions with an average KD of 3 x 10(-7) M. Binding of Zn2+ to this peptide results in a change in secondary structure as shown by circular dichroism spectroscopy. Biglycan, a proteoglycan that is structurally closely related to decorin contains a similar high affinity Zn2+-binding segment, whereas the structurally more distantly related proteoglycans, epiphycan and osteoglycin, do not bind Zn2+ with high affinity.
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------>authors=Yang, V. W-C, LaBrenz, S., Rosenberg, L., McQuillan, D., and Hook, M.
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------>updateTitle=Decorin is a Zn2+ metalloprotein.
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------>publish_year=1999
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A B C D E F G H I J K L M N O P Q R S T U V W X Y Z