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Article

Calcium Sensing by Recoverin: Effect of Protein Conformation on Ion Affinity.

The journal of physical chemistry letters - 5 Apr 2018

Timr Štěpán, Kadlec Jan, Srb Pavel, Ollila O H Samuli, Jungwirth Pavel

Abstract excerpt

The detailed functional mechanism of recoverin, which acts as a myristoyl switch at the rod outer-segment disk membrane, is elucidated by direct and replica-exchange molecular dynamics. In accord with NMR structural evidence and calcium binding assays, simulations point to the key role of enhanced calcium binding to the EF3 loop of the semiopen state of recoverin as compared to the closed state. This 2-4-order...

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Identifiers

PMID: 29537287
DOI: 10.1021/acs.jpclett.8b00495

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Calcium Sensing by Recoverin: Effect of Protein Conformation on Ion Affinity.PMID 29537287Read ↗

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A highly conserved cysteine of neuronal calcium-sensing proteins controls cooperative binding of Ca2+ to recoverin.Semantic proximity Read ↗

Functional restoration of the Ca2+-myristoyl switch in a recoverin mutant.Semantic proximity Read ↗

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Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase.Semantic proximity Read ↗

Intermotif Communication Induces Hierarchical Ca2+ Filling of Caldendrin.Semantic proximity Read ↗

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