Chemical shift assignments of retinal degeneration 3 protein (RD3)

  • Sunghyuk Lim
  • Diana Cudia
  • Qinhong Yu
  • Igor Peshenko
  • Alexander M. Dizhoor
  • James B. Ames
Article

Abstract

Retinal degeneration 3 protein (RD3) binds to retinal membrane guanylyl cyclase (RetGC) and suppresses the basal activity of RetGC in photoreceptor cells that opposes the allosteric activation of the cyclase by GCAP proteins. Mutations in RD3 that disrupt its inhibition of RetGC are implicated in human retinal degenerative disorders. Here we report both backbone and sidechain NMR assignments for the RD3 protein (BMRB accession no. 27305).

Keywords

Retinal degeneration protein 3 Retinal guanylyl cyclase RetGC RD3 GCAP 

Notes

Acknowledgements

We thank Jeff Walton for technical support and help with NMR experiments. Work supported by NIH Grants (EY012347) to J.B.A and (EY011522) to A.M.D.

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Copyright information

© Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  • Sunghyuk Lim
    • 1
  • Diana Cudia
    • 1
  • Qinhong Yu
    • 1
  • Igor Peshenko
    • 2
  • Alexander M. Dizhoor
    • 2
  • James B. Ames
    • 1
  1. 1.Department of ChemistryUniversity of CaliforniaDavisUSA
  2. 2.Department of Research, Pennsylvania College of OptometrySalus UniversityElkins ParkUSA

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