Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements
Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements
About this item
Full title
Author / Creator
Publisher
Switzerland: MDPI AG
Journal title
Language
English
Formats
Publication information
Publisher
Switzerland: MDPI AG
Subjects
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
Authors, Artists and Contributors
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