scholarly journals NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with 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 ◽  
...  
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.


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

Microbiology ◽  
2015 ◽  
Vol 161 (4) ◽  
pp. 895-902 ◽  
Author(s):  
Mouparna Dutta ◽  
Debasish Kar ◽  
Ankita Bansal ◽  
Sandeep Chakraborty ◽  
Anindya S. Ghosh

1993 ◽  
Vol 30 (18) ◽  
pp. 1671-1677 ◽  
Author(s):  
Krishna V. Kesari ◽  
Grada van Bleek ◽  
Stanley G. Nathenson ◽  
Jan Geliebter

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