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Article

NMR structural studies of human cystatin C dimers and monomers.

Journal of molecular biology - 15 Aug 1997

Ekiel I, Abrahamson M, Fulton D B, Lindahl P, Storer A C, Levadoux W, Lafrance M, Labelle S, Pomerleau Y, Groleau D, LeSauteur L, Gehring K

Abstract excerpt

Human cystatin C undergoes dimerization before unfolding. Dimerization leads to a complete loss of its activity as a cysteine proteinase inhibitor. A similar process of dimerization has been observed in cells, and may be related to the amyloid formation seen for the L68Q variant of the protein. Dimerization is barrier controlled, and no dimer/monomer interconversion can be observed at physiological conditions. As...

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PMID: 9268658
DOI: 10.1006/jmbi.1997.1150

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