Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent.

@article{Wearsch1997InteractionOE,
  title={Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent.},
  author={Pamela A. Wearsch and Christopher V Nicchitta},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 8},
  pages={5152-6}
}
GRP94, the endoplasmic reticulum paralog of hsp90, has recently been identified as a peptide and adenine nucleotide-binding protein. To determine if adenine nucleotides directly contribute to the regulation of GRP94 peptide binding activity, an in vitro peptide binding assay was developed. Using purified GRP94, we observed specific, saturable, temperature-sensitive binding of the peptide VSV8, a known in vivo ligand. ATP was without effect on VSV8 binding to GRP94, whether present during or… CONTINUE READING

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Peptide Binding by GRP94

  • Y. Miyata, I. Yahara
  • J. Biol
  • 1992

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