Cystine

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Cystine is formed by the oxidation of two proximal cysteine residues, covalently linking them in a disulfide bond.

Two cystines in human acid-beta-glucosidase (GlcCerase), the enzyme mutated in Gaucher disease, from 1ogs.


 

Disulfide Connectivity of Human beta-glucocerebrosidase, Cys4-Cys16&Cys18-Cys23 (1ogs)

Drag the structure with the mouse to rotate

Articles in Proteopedia concerning cystine include:


To view automatically seeded indices concerning cystine, see:

References and Notes


See Also

Additional Literature

  1. Ladenstein R, Ren B. Reconsideration of an early dogma, saying "there is no evidence for disulfide bonds in proteins from archaea". Extremophiles. 2008 Jan;12(1):29-38. Epub 2007 May 17. PMID:17508126 doi:10.1007/s00792-007-0076-z
  2. Dvir H, Harel M, McCarthy AA, Toker L, Silman I, Futerman AH, Sussman JL. X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease. EMBO Rep. 2003 Jul;4(7):704-9. PMID:12792654 doi:10.1038/sj.embor.embor873

External Resources

Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Eric Martz, Jaime Prilusky

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