4sod

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

RATIONAL DESIGN AND EXPRESSION OF A HEPARIN-TARGETED HUMAN SUPEROXIDE DISMUTASE

spinqualitylabelsall models 4sod Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed In order to improve the therapeutic effectiveness of human Cu,Zn superoxide dismutase (HSOD) by targeting it to cell surfaces and increasing its circulatory half-life, we have designed and expressed a heparin-binding derivative of HSOD. This design was based on the idea that structurally independent protein units, HSOD and the heparin-binding A+ helix from protein C inhibitor, could be combined with a carefully chosen linker, GlyProGly, to form a stable, bifunctional protein. The chimeric HSOD-GlyProGly-A+ protein was expressed and secreted to the periplasm of E. coli and had normal SOD activity. HSOD-GlyProGly-A+ had a significantly increased retention time relative to wild-type HSOD on a heparin affinity column, indicating that it was successfully targeted to heparin, and this binding was maintained at physiological ionic strength. When administered to mice, HSOD-GlyProGly-A+ had a half-life of approximately 15 minutes, twice that of wild-type HSOD. Our rational design approach should be generally applicable to the creation of bifunctional chimeric molecules. Rational design and expression of a heparin-targeted human superoxide dismutase.,Boissinot M, Kuhn LA, Lee P, Fisher CL, Wang Y, Hallewell RA, Tainer JA Biochem Biophys Res Commun. 1993 Jan 15;190(1):250-6. PMID:8422249 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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