Decorin Is a Zn2+ Metalloprotein
| Autor: | Vivian W C Yang, Lawrence C. Rosenberg, David J. McQuillan, Steven R. LaBrenz, Magnus Höök |
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| Rok vydání: | 1999 |
| Předmět: |
Protein Conformation
Decorin Recombinant Fusion Proteins Leucine-rich repeat Biochemistry Protein structure Biglycan Metalloproteins Metalloprotein Animals Amino Acid Sequence Binding site Molecular Biology chemistry.chemical_classification Extracellular Matrix Proteins Base Sequence biology Cell Biology Amino acid carbohydrates (lipids) Zinc Proteoglycan chemistry biology.protein Cattle Proteoglycans Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 274:12454-12460 |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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