Governing the monomer-dimer ratio of human cystatin C by single amino acid substitution in the hinge region

• Autorzy: Szymanska A. , Radulska A. , Czaplewska P. , Grubb A. , Grzonka Z. , Rodziewicz-Motowidlo S.
• Języki publikacji: EN

Abstrakty

EN

 Three dimensional domain swapping is one of the mechanisms involved in formation of insoluble aggregates of some amyloidogenic proteins. It has been proposed that proteins able to swap domains may share some common structural elements like conformationally constrained flexible turns/loops. We studied the role of loop L1 in the dimerization of human cystatin C using mutational analysis. Introduction of turn-favoring residues such as Asp or Asn into the loop sequence (in position 57) leads to a significant reduction of the dimer fraction in comparison with the wild type protein. On the other hand, introduction of a proline residue in position 57 leads to efficient dimer formation. Our results confirm the important role of the loop L1 in the dimerization process of human cystatin C and show that this process can be to some extent governed by single amino acid substitution.

Słowa kluczowe

PL

cystatin C; human cystatin C; dimerization; conformational tension; point mutation; amino acid; substitution; hinge region; dimerization process

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2009
• Tom: 56
• Numer: 3
• Opis fizyczny: p.455-463,fig.,ref.

Twórcy

autor

Szymanska A.

• University of Gdansk, J.Sobieskiego 18, 80-952 Gdansk, Poland

autor

Radulska A.

autor

Czaplewska P.

autor

Grubb A.

autor

Grzonka Z.

autor

Rodziewicz-Motowidlo S.

Bibliografia

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