NMR Structure of Retinal Guanylate Cyclase Activating Protein 5 (GCAP5) with R22A Mutation That Abolishes Dimerization and Enhances Cyclase Activation-Reference-Cited by-同舟云学术

NMR Structure of Retinal Guanylate Cyclase Activating Protein 5 (GCAP5) with R22A Mutation That Abolishes Dimerization and Enhances Cyclase Activation

Published:2024-04-25 Issue:10 Volume:63 Page:1246-1256
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cudia Diana L.¹,Ahoulou Effibe O.¹,Bej Aritra¹,Janssen Annika N.²,Scholten Alexander²,Koch Karl-W.²^ORCID,Ames James B.¹^ORCID

Affiliation:

1. Department of Chemistry, University of California, Davis, Davis, California 95616, United States

2. Division of Biochemistry, Department of Neuroscience, Carl von Ossietzky Universität Oldenburg, 26129 Oldenburg, Germany

Funder

Carl von Ossietzky Universit?t Oldenburg

National Eye Institute

Deutsche Forschungsgemeinschaft

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.4c00046

Reference58 articles.

1. Diversity of Guanylate Cyclase-Activating Proteins (GCAPs) in Teleost Fish: Characterization of Three Novel GCAPs (GCAP4, GCAP5, GCAP7) from Zebrafish (Danio rerio) and Prediction of Eight GCAPs (GCAP1-8) in Pufferfish (Fugu rubripes)

2. Structural Characterization of Ferrous Ion Binding to Retinal Guanylate Cyclase Activator Protein 5 from Zebrafish Photoreceptors

3. Expression profiles of three novel sensory guanylate cyclases and guanylate cyclase-activating proteins in the zebrafish retina

4. The human photoreceptor membrane guanylyl cyclase, RetGC, is present in outer segments and is regulated by calcium and a soluble activator

5. Cloning and expression of a second photoreceptor-specific membrane retina guanylyl cyclase (RetGC), RetGC-2.