Back to Search
Start Over
Oligomeric Structural Transition of HspB1 from Chinese Hamster
- Source :
- International Journal of Molecular Sciences, Volume 22, Issue 19, International Journal of Molecular Sciences, Vol 22, Iss 10797, p 10797 (2021)
- Publication Year :
- 2021
- Publisher :
- MDPI, 2021.
-
Abstract
- HspB1 is a mammalian sHsp that is ubiquitously expressed in almost all tissues and involved in regulating many vital functions. Although the recent crystal structure of human HspB1 showed that 24 monomers form the oligomeric complex of human HspB1 in a spherical configuration, the molecular architecture of HspB1 is still controversial. In this study, we examined the oligomeric structural change of CgHspB1 by sedimentation velocity analytical ultracentrifugation. At the low temperature of 4 °C, CgHspB1 exists as an 18-mer, probably a trimeric complex of hexamers. It is relatively unstable and partially dissociates into small oligomers, hexamers, and dodecamers. At elevated temperatures, the 24-mer was more stable than the 18-mer. The 24-mer is also in dynamic equilibrium with the dissociated oligomers in the hexameric unit. The hexamer further dissociates to dimers. The disulfide bond between conserved cysteine residues seems to be partly responsible for the stabilization of hexamers. The N-terminal domain is involved in the assembly of dimers and the interaction between hexamers. It is plausible that CgHspB1 expresses a chaperone function in the 24-mer structure.
- Subjects :
- folding
animal structures
QH301-705.5
Protein Conformation
Crystal structure
CHO Cells
Random hexamer
Chinese hamster
Catalysis
Article
Inorganic Chemistry
chemistry.chemical_compound
Cricetulus
Protein Domains
Cricetinae
chaperone
Animals
Humans
Physical and Theoretical Chemistry
Biology (General)
Molecular Biology
QD1-999
Spectroscopy
Dynamic equilibrium
Heat-Shock Proteins
biology
Chemistry
Organic Chemistry
General Medicine
small heat shock protein
Computer Science Applications
Folding (chemistry)
Monomer
Structural change
Chaperone (protein)
biology.protein
Biophysics
Protein Multimerization
analytical ultracentrifugation
Cysteine
Molecular Chaperones
Subjects
Details
- Language :
- English
- ISSN :
- 14220067
- Volume :
- 22
- Issue :
- 19
- Database :
- OpenAIRE
- Journal :
- International Journal of Molecular Sciences
- Accession number :
- edsair.doi.dedup.....d5b1a2696cfe4b684de944e5714da095