Sandbox Reserved 164

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This Sandbox is Reserved from March 9, 2011, through May 30, 2011 for use by the course Biochemistry at Reinhardt University, Waleska, USA, taught by Irma Santoro. This reservation includes Sandbox Reserved 162 through Sandbox Reserved 168.
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SOD 1 protein NMR

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Contents

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 [1]. This occurs in a quick two step mechanism 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 [2].


Structure

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[3].

ALS

References

  1. ↑ McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049-55. PMID:5389100
  2. ↑ SOD 1. Genetics Home Reference. U.S. National Library of Medicine; 2010
  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


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

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