PUBLICATION
Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation
- Authors
- Cudia, D., Ahoulou, E.O., Ames, J.B.
- ID
- ZDB-PUB-230503-37
- Date
- 2023
- Source
- Biomolecular NMR assignments 17(1): 115-119 (Journal)
- Registered Authors
- Keywords
- EF-hand, GCAP5, Phototransduction, R22A, Retinal guanylyl cyclase
- MeSH Terms
-
- Zebrafish/metabolism
- Animals
- Guanylate Cyclase*/chemistry
- Guanylate Cyclase*/genetics
- Guanylate Cyclase*/metabolism
- Dimerization
- Mutation
- Guanylate Cyclase-Activating Proteins*/chemistry
- Nuclear Magnetic Resonance, Biomolecular
- Calcium/metabolism
- PubMed
- 37129703 Full text @ Biomol. NMR Assign.
Citation
Cudia, D., Ahoulou, E.O., Ames, J.B. (2023) Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation. Biomolecular NMR assignments. 17(1):115-119.
Abstract
Retinal membrane guanylyl cyclases (RetGCs) in vertebrate rod and cone photoreceptors are activated by a family of neuronal Ca2+ sensor proteins called guanylyl cyclase activating proteins (GCAP1-7). GCAP5 from zebrafish photoreceptors binds to RetGC and confers Ca2+/Fe2+-dependent regulation of RetGC enzymatic activity that promotes the recovery phase of visual phototransduction. We report NMR chemical shift assignments of GCAP5 with a R22A mutation (called GCAP5R22A) that abolishes protein dimerization and activates RetGC with 3-fold higher activity than that of wild type GCAP5 (BMRB No. 51,783).
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping