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

2009 ◽  
Vol 56 (3) ◽  
Author(s):  
Aneta Szymańska ◽  
Adrianna Radulska ◽  
Paulina Czaplewska ◽  
Anders Grubb ◽  
Zbigniew Grzonka ◽  
...  

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.

FEBS Journal ◽  
2019 ◽  
Vol 287 (2) ◽  
pp. 361-376 ◽  
Author(s):  
Martyna Maszota‐Zieleniak ◽  
Przemyslaw Jurczak ◽  
Marta Orlikowska ◽  
Igor Zhukov ◽  
Dominika Borek ◽  
...  

Biopolymers ◽  
2009 ◽  
Vol 91 (5) ◽  
pp. 373-383 ◽  
Author(s):  
Sylwia Rodziewicz-Motowidło ◽  
Justyna Iwaszkiewicz ◽  
Renata Sosnowska ◽  
Paulina Czaplewska ◽  
Emil Sobolewski ◽  
...  

2001 ◽  
Vol 82 (9) ◽  
pp. 2169-2172 ◽  
Author(s):  
Naoko Nakagawa ◽  
Ritsuko Kubota ◽  
Toshimasa Nakagawa ◽  
Yoshinobu Okuno

To study the neutralizing epitopes of influenza B virus Victoria group strains, two monoclonal antibodies (MAbs) were used to select antigenic variants of the virus. MAbs 10B8 and 8E6 were found to react with B/Victoria group strains in three tests, peroxidase–antiperoxidase staining, haemagglutination inhibition and neutralization tests; no reactivity with B/Yamagata group strains was observed. Analysis of the deduced amino acid sequences of 10B8-induced variants identified a single amino acid deletion at residue 165 or 170, as well as a single amino acid substitution at residues 164 (Asp→Tyr), 165 (Asn→Ser or Thr) or 203 (Lys→Thr or Asn). A single amino acid substitution at residue 241 (Pro→Ser) was observed in 8E6-induced variants. Three-dimensional analysis showed that the epitopes for both MAbs were situated in close proximity to each other. Since B/Yamagata group strains are characterized by amino acid deletions at residues 164–166, the epitope for MAb 10B8 is strictly specific for B/Victoria group strains.


1996 ◽  
Vol 5 (3) ◽  
pp. 542-545 ◽  
Author(s):  
Kunihiko Gekko ◽  
Youjiro Tamura ◽  
Eiji Ohmae ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document