Chemical shift assignments of retinal degeneration 3 protein (RD3)

Sunghyuk Lim; Diana Cudia; Qinhong Yu; Igor Peshenko; Alexander M Dizhoor; James B Ames

doi:10.1007/s12104-018-9802-y

Chemical shift assignments of retinal degeneration 3 protein (RD3)

Biomol NMR Assign. 2018 Apr;12(1):167-170. doi: 10.1007/s12104-018-9802-y. Epub 2018 Jan 11.

Authors

Sunghyuk Lim¹, Diana Cudia¹, Qinhong Yu¹, Igor Peshenko², Alexander M Dizhoor², James B Ames³

Affiliations

¹ Department of Chemistry, University of California, Davis, CA, 95616, USA.
² Department of Research, Pennsylvania College of Optometry, Salus University, Elkins Park, PA, 19027, USA.
³ Department of Chemistry, University of California, Davis, CA, 95616, USA. jbames@ucdavis.edu.

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: GCAP; RD3; RetGC; Retinal degeneration protein 3; Retinal guanylyl cyclase.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Eye Proteins / chemistry*
Humans
Nuclear Magnetic Resonance, Biomolecular*

Substances

Eye Proteins
RD3 protein, human

Abstract

Publication types

MeSH terms

Substances

Grants and funding