Article
The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants.
Biopolymers - 1 May 2009
Rodziewicz-Motowidło Sylwia, Iwaszkiewicz Justyna, Sosnowska Renata, Czaplewska Paulina, Sobolewski Emil, Szymańska Aneta, Stachowiak Krystyna, Liwo Adam
Abstract excerpt
Human cystatin C (HCC) is one of the amyloidogenic proteins to be shown to oligomerize via a three-dimensional domain swapping mechanism. This process precedes the formation of a stable dimer and proceeds particularly easily in the case of the L68Q mutant. According to the proposed mechanism, dimerization of the HCC precedes conformational changes within the beta2 and beta3 strands. In this article, we present...
Topics
- Amino Acid Sequence
- Circular Dichroism
- Cystatin C
- Humans
- Models, Molecular
- Molecular Sequence Data
- Mutant Proteins
- Mutation
- Protein Structure, Secondary
- Structure-Activity Relationship
- Thermodynamics
- Valine