Sandbox Reserved 164: Difference between revisions

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== Superoxide Dismutase 1 (SOD1) ==
== Superoxide Dismutase 1 (SOD 1) ==
SOD1 is one of three oxidoreductase enzymes that is responsible for binding copper and zinc ions to highly reactive oxygen free radicals and transforming them into oxygen and hydrogen peroxide <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref>.  This protein is coded for by the SOD 1 gene located on chromosome 21 at position 21q22.1 from base pairs 33,031,934 to 33,041,243 <ref name="Sod1">SOD 1.  Genetics Home Reference.  U.S. National Library of Medicine; 2010</ref>.
SOD1 is one of three oxidoreductase enzymes that is responsible for binding copper and zinc ions to highly reactive oxygen free radicals and transforming them into oxygen and hydrogen peroxide <ref name="McCord">McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100</ref>.  This protein is coded for by the SOD 1 gene located on chromosome 21 at position 21q22.1 from base pairs 33,031,934 to 33,041,243 <ref name="Sod1">SOD 1.  Genetics Home Reference.  U.S. National Library of Medicine; 2010</ref>.




== Structure ==
== Structure ==
The SOD 1 protein has an amino acid sequence of 154 AA.
The SOD 1 protein is a homodimer with an amino acid sequence length of 154.  SOD 1 has an 8-stranded "Greek key" beta-barrel shape with the active site located between the barrels.  ligands of the copper and zinc are six histidine and one aspartate side-chains; one histidine is shared between the two metals<ref name="Tainer">Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150</ref>.


== ALS ==
== ALS ==
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2. McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med. 1988;5(5-6):363-9. PMID:2855736
2. McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med. 1988;5(5-6):363-9. PMID:2855736
3. Tainer JA, Getzoff ED, Richardson JS, Richardson DC. Structure and mechanism of copper, zinc superoxide dismutase. Nature. 1983 Nov 17-23;306(5940):284-7. PMID:6316150