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. D...
Topics
- Amino Acid Sequence
- Cystatin C
- Cystatins
- Cysteine Proteinase Inhibitors
- Diffusion
- Dimerization
- Genetic Variation
- Humans
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Models, Structural
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Point Mutation
- Protein Conformation