Human MnSOD and Cancer Research: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 8: Line 8:


== Structure ==
== Structure ==
Human Superoxide Dismutase (MnSOD) is a 22kD homotetrameric protein that is characterized by each subunit containing an N-terminus helical hairpin and alpha/beta domain that contribute to the catalytic site, the enzyme has four manganese active sites <ref name="Borgstahl et al">PMID:1394426</ref>. MnSOD alpha and beta C-terminus domains contain a “...three stranded antiparallel beta-sheet and five alpha-helices” <ref name="Borgstahl et al">PMID:1394426</ref>. The N-terminus helical hairpins are composed of “...two long antiparallel alpha-helices separated by a tight turn to form a helical hairpin” <ref name="Borgstahl et al">PMID:1394426</ref>. The active sites themselves are positioned between the helical and beta-sheet areas, while also joining the two domains <ref name="Borgstahl et al">PMID:1394426</ref>. A couple of amino acid residues from both domains and a water molecule are responsible for the ligation of Manganese <ref name="Borgstahl et al">PMID:1394426</ref>. The four active sites associate in pairs on either side of the enzyme.
Human Superoxide Dismutase (MnSOD) is a 22kD homotetrameric protein that is characterized by each subunit containing an <scene name='81/814062/N-terminus_structure/1'>N-terminus helical hairpin</scene> and alpha/beta domain that contribute to the catalytic site, the enzyme has four manganese active sites <ref name="Borgstahl et al">PMID:1394426</ref>. MnSOD alpha and beta C-terminus domains contain a “...three stranded antiparallel beta-sheet and five alpha-helices” <ref name="Borgstahl et al">PMID:1394426</ref>. The N-terminus helical hairpins are composed of “...two long antiparallel alpha-helices separated by a tight turn to form a helical hairpin” <ref name="Borgstahl et al">PMID:1394426</ref>. The active sites themselves are positioned between the helical and beta-sheet areas, while also joining the two domains <ref name="Borgstahl et al">PMID:1394426</ref>. A couple of amino acid residues from both domains and a water molecule are responsible for the ligation of Manganese <ref name="Borgstahl et al">PMID:1394426</ref>. The four active sites associate in pairs on either side of the enzyme.




Retrieved from "https://proteopedia.org/Human_MnSOD_and_Cancer_Research"