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2009 | 56 | 3 | 455-463
Article title

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

Content
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EN
Abstracts
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.
Year
Volume
56
Issue
3
Pages
455-463
Physical description
Dates
published
2009
received
2009-05-14
revised
2009-07-02
accepted
2009-07-22
(unknown)
2009-07-27
References
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Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv56p455kz
Identifiers
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