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

Contents

Visualization

FirstGlance in Jmol displays all cystines (disulfide bonds) in any given protein in a clear manner. To display a protein in FirstGlance and see its disulfide bonds:

  • Find a page in Proteopedia about that protein. You can use the search slot at left to search for the name of the protein, or a specific PDB code.
  • If the page is not titled with a PDB code, look for mention of a PDB code, and go to the page titled with that PDB code.
  • Click on the link FirstGlance beneath the molecule.
  • Once you see the protein in FirstGlance, click on More Views.., then on Disulfide bonds: show all.

Eventually, you will be able to select and display disulfide bonds in Proteopedia's Scene Authoring Tools (SAT). In March, 2012, this is on the Wishlist. Currently, in the SAT, you can select CYS, which includes both cysteine and cystine.

Articles

Articles in Proteopedia concerning cystine include:

Cystine Categories

To view automatically seeded "Category" indices concerning cystine, see:

References and Notes


See Also

Additional Literature

  • 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
  • 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?)

Eric Martz, Wayne Decatur, Jaime Prilusky

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