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Structural and functional characterization of interactions between the dihydropyridine receptor II-III loop and the ryanodine receptor

Casarotto, Marco; Cui, Yan Fang; Karunasekara, Yamuna; Harvey, Peta; Norris, Nicole; Board, Philip; Dulhunty, Angela

Description

1. Excitation-contraction coupling in skeletal muscle is dependent on a physical interaction between the dihydropyridine receptor (DHPR) and the ryanodine receptor (RyR). 2. A number of peptides derived from the II-III loop region of the DHPR have been shown to be functionally active in stimulating the release of calcium via RyR channels. Their function has been found to correlate with the presence of a basic helical region located at the N-terminus of the II-III loop. 3. The entire recombinant...[Show more]

dc.contributor.authorCasarotto, Marco
dc.contributor.authorCui, Yan Fang
dc.contributor.authorKarunasekara, Yamuna
dc.contributor.authorHarvey, Peta
dc.contributor.authorNorris, Nicole
dc.contributor.authorBoard, Philip
dc.contributor.authorDulhunty, Angela
dc.date.accessioned2015-12-07T22:24:52Z
dc.identifier.issn0305-1870
dc.identifier.urihttp://hdl.handle.net/1885/21018
dc.description.abstract1. Excitation-contraction coupling in skeletal muscle is dependent on a physical interaction between the dihydropyridine receptor (DHPR) and the ryanodine receptor (RyR). 2. A number of peptides derived from the II-III loop region of the DHPR have been shown to be functionally active in stimulating the release of calcium via RyR channels. Their function has been found to correlate with the presence of a basic helical region located at the N-terminus of the II-III loop. 3. The entire recombinant skeletal DHPR II-III loop is an efficient activator of RyR1 and RyR2. 4. The skeletal DHPR II-III loop is comprised of a series of a-helices, but its tertiary structure has been determined to be unstructured and flexible. 5. Fluorescence quenching experiments have been used to identify and measure the binding affinity of the II-III loop with fragments of the RyR.
dc.publisherBlackwell Science Asia
dc.sourceClinical and Experimental Pharmacology and Physiology
dc.subjectKeywords: 1,4 dihydropyridine receptor; ryanodine receptor; alpha helix; amino terminal sequence; binding affinity; calcium transport; conference paper; excitation contraction coupling; protein protein interaction; skeletal muscle; Binding Sites; Calcium Channels, Dihydropyridine receptor; Excitation-contraction coupling; II-III loop; Nuclear magnetic resonance; Protein-protein interaction; Ryanodine receptor
dc.titleStructural and functional characterization of interactions between the dihydropyridine receptor II-III loop and the ryanodine receptor
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume33
dc.date.issued2006
local.identifier.absfor060601 - Animal Physiology - Biophysics
local.identifier.ariespublicationu4020362xPUB15
local.type.statusPublished Version
local.contributor.affiliationCasarotto, Marco, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationCui, Yan Fang, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationKarunasekara, Yamuna, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHarvey, Peta, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationNorris, Nicole, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBoard, Philip, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationDulhunty, Angela, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue11
local.bibliographicCitation.startpage1114
local.bibliographicCitation.lastpage17
local.identifier.doi10.1111/j.1440-1681.2006.04501.x
dc.date.updated2015-12-07T09:29:33Z
local.identifier.scopusID2-s2.0-33750087518
CollectionsANU Research Publications

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