ISSN:
1573-4978
Keywords:
eye lens
;
molecular chaperone
;
mouse HSP25
;
α-crystallin
;
stress proteins
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The C-terminal domain and tail, which is the most conserved region of the α-crystallin/small heat shock protein (HSP) family, was obtained from rat αA-crystallin, bovine αB-crystallin and mouse HSP25. All three domains have primarily β-sheet conformation and less than 10% of α-helix, like the proteins from which they are derived. Whereas the C-terminal part of αA-crystallin forms dimers or tetramers, the corresponding regions of αB-crystallin and HSP25 form larger aggregates. The heat-protective activity, recently described for the α-crystallin/small HSP family, is not retained in the C-terminal domain and tail. In the course of this study some differences with the previously published sequence of HSP25 were observed, and a revision is proposed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01674432
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