Kb. Merck et al., COMPARISON OF THE HOMOLOGOUS CARBOXY-TERMINAL DOMAIN AND TAIL OF ALPHA-CRYSTALLIN AND SMALL HEAT-SHOCK PROTEIN, Molecular biology reports, 18(3), 1993, pp. 209-215
The C-terminal domain and tail, which is the most conserved region of
the alpha-crystallin/small heat shock protein (HSP) family, was obtain
ed from rat alphaA-crystallin, bovine alphaB-crystallin and mouse HSP2
5. All three domains have primarily beta-sheet conformation and less t
han 10% of alpha-helix, like the proteins from which they are derived.
Whereas the C-terminal part of alphaA-crystallin forms dimer or tetra
mers, the corresponding regions for the alpha-crystallin/small HSP fam
ily, 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.