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Human PRPH2-ROM1 hetero-dimer


ABSTRACT:

SUBMITTER: Dounia El Mazouni 

PROVIDER: EMPIAR-11482 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

Cryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis.

El Mazouni Dounia D   Gros Piet P  

Science advances 20221109 45


Mammalian peripherin-2 (PRPH2) and rod outer segment membrane protein 1 (ROM1) are retina-specific tetraspanins that partake in the constant renewal of stacked membrane discs of photoreceptor cells that enable vision. Here, we present single-particle cryo-electron microscopy structures of solubilized PRPH2-ROM1 heterodimers and higher-order oligomers. High-risk PRPH2 and ROM1 mutations causing blindness map to the protein-dimer interface. Cysteine bridges connect dimers forming positive-curved o  ...[more]

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