The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology.

@article{Morshauser1995ThePD,
  title={The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology.},
  author={R C Morshauser and Hsin Wang and Gregory C. Flynn and Erik R.P. Zuiderweg},
  journal={Biochemistry},
  year={1995},
  volume={34 19},
  pages={6261-6}
}
Modern NMR methods were used to determine the secondary structure topology of the 18 kDa peptide binding domain of the chaperone protein Hsc70 in solution. This report constitutes the first experimental conformational information on this important domain of the class of Hsp70 proteins. The domain consists of two four-stranded antiparallel beta-sheets and a single alpha-helix. The topology does not resemble at all the topology observed in the human leukocyte antigen (HLA) proteins of the major… CONTINUE READING
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