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Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements

Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10219436

Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements

About this item

Full title

Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements

Publisher

Switzerland: MDPI AG

Journal title

International journal of molecular sciences, 2023-05, Vol.24 (10), p.8903

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

Arrestin-1, or visual arrestin, exhibits an exquisite selectivity for light-activated phosphorylated rhodopsin (P-Rh*) over its other functional forms. That selectivity is believed to be mediated by two well-established structural elements in the arrestin-1 molecule, the activation sensor detecting the active conformation of rhodopsin and the phosp...

Alternative Titles

Full title

Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10219436

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10219436

Other Identifiers

ISSN

1422-0067,1661-6596

E-ISSN

1422-0067

DOI

10.3390/ijms24108903

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