Overall conformation of covalently stabilized domain-swapped dimer of human cystatin C in solution
Murawska, Magdalena ; Szymańska, Aneta ; Grubb, Anders LU
and Kozak, Maciej
(2017)
In Nuclear Instruments and Methods in Physics Research, Section B: Beam Interactions with Materials and Atoms
411.
p.136-140
- Abstract
Human cystatin C (HCC), a small protein, plays a crucial role in inhibition of cysteine proteases. The most common structural form of human cystatin C in crystals is a dimer, which has been evidenced both for the native protein and its mutants. In these structures, HCC dimers were formed through the mechanism of domain swapping. The structure of the monomeric form of human cystatin C was determined for V57N mutant and the mutant with the engineered disulfide bond (L47C)–(G69C) (known as stab1-HCC). On the basis of stab1-HCC, a number of covalently stabilized oligomers, including also dimers have been obtained. The aim of this study was to analyze the structure of the covalently stabilized dimer HCC in solution by the small angle X-ray... (More)
Human cystatin C (HCC), a small protein, plays a crucial role in inhibition of cysteine proteases. The most common structural form of human cystatin C in crystals is a dimer, which has been evidenced both for the native protein and its mutants. In these structures, HCC dimers were formed through the mechanism of domain swapping. The structure of the monomeric form of human cystatin C was determined for V57N mutant and the mutant with the engineered disulfide bond (L47C)–(G69C) (known as stab1-HCC). On the basis of stab1-HCC, a number of covalently stabilized oligomers, including also dimers have been obtained. The aim of this study was to analyze the structure of the covalently stabilized dimer HCC in solution by the small angle X-ray scattering (SAXS) technique and synchrotron radiation. Experimental data confirmed that in solution this protein forms a dimer, which is characterized by the radius of gyration RG = 3.1 nm and maximum intramolecular distance Dmax = 10.3 nm. Using the ab initio method and program DAMMIN, we propose a low resolution structure of stabilized covalently cystatin C in solution. Stab-HCC dimer adopts in solution an elongated conformation, which is well reconstructed by the ab initio model.
(Less)
- author
- Murawska, Magdalena
; Szymańska, Aneta
; Grubb, Anders
LU
and Kozak, Maciej
- publishing date
- 2017-11-15
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Human cystatin C, Shape determination, Small angle X-ray scattering, Synchrotron radiation
- in
- Nuclear Instruments and Methods in Physics Research, Section B: Beam Interactions with Materials and Atoms
- volume
- 411
- pages
- 5 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:85014678969
- ISSN
- 0168-583X
- DOI
- 10.1016/j.nimb.2017.02.090
- language
- English
- LU publication?
- no
- id
- b646da39-771c-4105-b100-dec12cc3d6d2
- date added to LUP
- 2017-11-22 08:47:45
- date last changed
- 2023-01-07 03:07:24
@article{b646da39-771c-4105-b100-dec12cc3d6d2,
abstract = {{<p>Human cystatin C (HCC), a small protein, plays a crucial role in inhibition of cysteine proteases. The most common structural form of human cystatin C in crystals is a dimer, which has been evidenced both for the native protein and its mutants. In these structures, HCC dimers were formed through the mechanism of domain swapping. The structure of the monomeric form of human cystatin C was determined for V57N mutant and the mutant with the engineered disulfide bond (L47C)–(G69C) (known as stab1-HCC). On the basis of stab1-HCC, a number of covalently stabilized oligomers, including also dimers have been obtained. The aim of this study was to analyze the structure of the covalently stabilized dimer HCC in solution by the small angle X-ray scattering (SAXS) technique and synchrotron radiation. Experimental data confirmed that in solution this protein forms a dimer, which is characterized by the radius of gyration R<sub>G</sub> = 3.1 nm and maximum intramolecular distance D<sub>max</sub> = 10.3 nm. Using the ab initio method and program DAMMIN, we propose a low resolution structure of stabilized covalently cystatin C in solution. Stab-HCC dimer adopts in solution an elongated conformation, which is well reconstructed by the ab initio model.</p>}},
author = {{Murawska, Magdalena and Szymańska, Aneta and Grubb, Anders and Kozak, Maciej}},
issn = {{0168-583X}},
keywords = {{Human cystatin C; Shape determination; Small angle X-ray scattering; Synchrotron radiation}},
language = {{eng}},
month = {{11}},
pages = {{136--140}},
publisher = {{Elsevier}},
series = {{Nuclear Instruments and Methods in Physics Research, Section B: Beam Interactions with Materials and Atoms}},
title = {{Overall conformation of covalently stabilized domain-swapped dimer of human cystatin C in solution}},
url = {{http://dx.doi.org/10.1016/j.nimb.2017.02.090}},
doi = {{10.1016/j.nimb.2017.02.090}},
volume = {{411}},
year = {{2017}},
}