Interactions within the coiled-coil domain of RetGC-1 guanylyl cyclase are optimized for regulation rather than for high affinity.

@article{Ramamurthy2001InteractionsWT,
  title={Interactions within the coiled-coil domain of RetGC-1 guanylyl cyclase are optimized for regulation rather than for high affinity.},
  author={Visvanathan Ramamurthy and Chandra Tucker and Susan E. Wilkie and Valerie Daggett and Debbie M. Hunt and James B Hurley},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 28},
  pages={26218-29}
}
RetGC-1, a member of the membrane guanylyl cyclase family of proteins, is regulated in photoreceptor cells by a Ca(2+)-binding protein known as GCAP-1. Proper regulation of RetGC-1 is essential in photoreceptor cells for normal light adaptation and recovery to the dark state. In this study we show that cGMP synthesis by RetGC-1 requires dimerization, because critical functions in the catalytic site must be provided by each of the two polypeptide chains of the dimer. We also show that an intact… CONTINUE READING
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