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

Szymańska, Aneta ; Radulska, Adrianna ; Czaplewska, Paulina ; Grubb, Anders LU orcid ; Grzonka, Zbigniew and Rodziewicz-Motowidło, Sylwia (2009) In Acta Biochimica Polonica 56(3). p.455-463
Abstract
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... (More)
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. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Amino Acid Substitution, Chromatography, Gel, Circular Dichroism, Cystatin C, Electrophoresis, Humans, Mutagenesis, Site-Directed, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Structure-Activity Relationship, Journal Article, Research Support, Non-U.S. Gov't
in
Acta Biochimica Polonica
volume
56
issue
3
pages
9 pages
publisher
Frontiers Media S. A.
external identifiers
  • wos:000270660500011
  • scopus:74049084604
  • pmid:19636441
ISSN
0001-527X
language
English
LU publication?
yes
id
a694617f-7b17-42f1-b65e-ef31667f2485 (old id 1507689)
date added to LUP
2016-04-01 15:04:36
date last changed
2025-02-28 13:58:47
@article{a694617f-7b17-42f1-b65e-ef31667f2485,
  abstract     = {{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.}},
  author       = {{Szymańska, Aneta and Radulska, Adrianna and Czaplewska, Paulina and Grubb, Anders and Grzonka, Zbigniew and Rodziewicz-Motowidło, Sylwia}},
  issn         = {{0001-527X}},
  keywords     = {{Amino Acid Substitution; Chromatography, Gel; Circular Dichroism; Cystatin C; Electrophoresis; Humans; Mutagenesis, Site-Directed; Protein Multimerization; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Journal Article; Research Support, Non-U.S. Gov't}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{455--463}},
  publisher    = {{Frontiers Media S. A.}},
  series       = {{Acta Biochimica Polonica}},
  title        = {{Governing the monomer-dimer ratio of human cystatin C by single amino acid substitution in the hinge region}},
  volume       = {{56}},
  year         = {{2009}},
}