Unknown

Dataset Information

0

Single particle cryo-EM of the complex between interphotoreceptor retinoid-binding protein and a monoclonal antibody.


ABSTRACT: Interphotoreceptor retinoid-binding protein (IRBP) is a highly expressed protein secreted by rod and cone photoreceptors that has major roles in photoreceptor homeostasis as well as retinoid and polyunsaturated fatty acid transport between the neural retina and retinal pigment epithelium. Despite two crystal structures reported on fragments of IRBP and decades of research, the overall structure of IRBP and function within the visual cycle remain unsolved. Here, we studied the structure of native bovine IRBP in complex with a monoclonal antibody (mAb5) by cryo-electron microscopy, revealing the tertiary and quaternary structure at sufficient resolution to clearly identify the complex components. Complementary mass spectrometry experiments revealed the structure and locations of N-linked carbohydrate post-translational modifications. This work provides insight into the structure of IRBP, displaying an elongated, flexible three-dimensional architecture not seen among other retinoid-binding proteins. This work is the first step in elucidation of the function of this enigmatic protein.

SUBMITTER: Sears AE 

PROVIDER: S-EPMC7589273 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Single particle cryo-EM of the complex between interphotoreceptor retinoid-binding protein and a monoclonal antibody.

Sears Avery E AE   Albiez Stefan S   Gulati Sahil S   Wang Benlian B   Kiser Philip P   Kovacik Lubomir L   Engel Andreas A   Stahlberg Henning H   Palczewski Krzysztof K  

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 20200828 10


Interphotoreceptor retinoid-binding protein (IRBP) is a highly expressed protein secreted by rod and cone photoreceptors that has major roles in photoreceptor homeostasis as well as retinoid and polyunsaturated fatty acid transport between the neural retina and retinal pigment epithelium. Despite two crystal structures reported on fragments of IRBP and decades of research, the overall structure of IRBP and function within the visual cycle remain unsolved. Here, we studied the structure of native  ...[more]

Similar Datasets

| S-EPMC6009202 | biostudies-literature
| S-EPMC7611073 | biostudies-literature
| S-EPMC5886813 | biostudies-literature
| S-EPMC7285653 | biostudies-literature
| S-EPMC4355169 | biostudies-literature
| S-EPMC6760665 | biostudies-literature
| S-EPMC7779749 | biostudies-literature
| S-EPMC7337043 | biostudies-literature
| EMPIAR-11832 | biostudies-other