4sod: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
{{Theoretical_model}} | |||
==RATIONAL DESIGN AND EXPRESSION OF A HEPARIN-TARGETED HUMAN SUPEROXIDE DISMUTASE== | |||
<StructureSection load='4sod' size='340' side='right'caption='[[4sod]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4SOD FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4sod FirstGlance], [https://www.ebi.ac.uk/pdbsum/4sod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4sod ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:8422249</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4sod" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Fisher, C L]] | |||
[[Category: Kuhn, L A]] | |||
[[Category: Tainer, J A]] | |||
Latest revision as of 10:43, 15 March 2023
 |
RATIONAL DESIGN AND EXPRESSION OF A HEPARIN-TARGETED HUMAN SUPEROXIDE DISMUTASE
| ||||||||||||
