Matches in SemOpenAlex for { <https://semopenalex.org/work/W2953298276> ?p ?o ?g. }
Showing items 1 to 76 of
76
with 100 items per page.
- W2953298276 abstract "To characterize the conformational dynamics of sarcoplasmic reticulum (SR) calcium pump (SERCA) we performed molecular dynamics simulations beginning with several different high-resolution structures. We quantified differences in structural disorder and dynamics for an open conformation of SERCA versus closed structures and observed that dynamic motions of SERCA cytoplasmic domains decreased with decreasing domain–domain separation distance. The results are useful for interpretation of recent intramolecular Forster resonance energy transfer (FRET) distance measurements obtained for SERCA fused to fluorescent protein tags. Those previous physical measurements revealed several discrete structural substates and suggested open conformations of SERCA are more dynamic than compact conformations. The present simulations support this hypothesis and provide additional details of SERCA molecular mechanisms. Specifically, all-atoms simulations revealed large-scale translational and rotational motions of the SERCA N-domain relative to the A- and P-domains during the transition from an open to a closed headpiece conformation over the course of a 400 ns trajectory. The open-to-closed structural transition was accompanied by a disorder-to-order transition mediated by an initial interaction of an N-domain loop (Nβ5-β6, residues 426–436) with residues 133–139 of the A-domain. Mutation of three negatively charged N-domain loop residues abolished the disorder-to-order transition and prevented the initial domain–domain interaction and subsequent closure of the cytoplasmic headpiece. Coarse-grained molecular dynamics simulations were in harmony with all-atoms simulations and physical measurements and revealed a close communication between fluorescent protein tags and the domain to which they were fused. The data indicate that previous intramolecular FRET distance measurements report SERCA structure changes with high fidelity and suggest a structural mechanism that facilitates the closure of the SERCA cytoplasmic headpiece." @default.
- W2953298276 created "2019-06-27" @default.
- W2953298276 creator A5003533945 @default.
- W2953298276 creator A5068004698 @default.
- W2953298276 date "2015-01-01" @default.
- W2953298276 modified "2023-09-26" @default.
- W2953298276 title "A Structural Mechanism for Calcium Transporter Headpiece Closure" @default.
- W2953298276 hasPublicationYear "2015" @default.
- W2953298276 type Work @default.
- W2953298276 sameAs 2953298276 @default.
- W2953298276 citedByCount "0" @default.
- W2953298276 crossrefType "journal-article" @default.
- W2953298276 hasAuthorship W2953298276A5003533945 @default.
- W2953298276 hasAuthorship W2953298276A5068004698 @default.
- W2953298276 hasConcept C121332964 @default.
- W2953298276 hasConcept C12554922 @default.
- W2953298276 hasConcept C147597530 @default.
- W2953298276 hasConcept C159467904 @default.
- W2953298276 hasConcept C181199279 @default.
- W2953298276 hasConcept C185592680 @default.
- W2953298276 hasConcept C23265538 @default.
- W2953298276 hasConcept C2781414619 @default.
- W2953298276 hasConcept C55493867 @default.
- W2953298276 hasConcept C59593255 @default.
- W2953298276 hasConcept C62520636 @default.
- W2953298276 hasConcept C71240020 @default.
- W2953298276 hasConcept C75079739 @default.
- W2953298276 hasConcept C8010536 @default.
- W2953298276 hasConcept C86803240 @default.
- W2953298276 hasConcept C91881484 @default.
- W2953298276 hasConcept C935647 @default.
- W2953298276 hasConcept C96305047 @default.
- W2953298276 hasConceptScore W2953298276C121332964 @default.
- W2953298276 hasConceptScore W2953298276C12554922 @default.
- W2953298276 hasConceptScore W2953298276C147597530 @default.
- W2953298276 hasConceptScore W2953298276C159467904 @default.
- W2953298276 hasConceptScore W2953298276C181199279 @default.
- W2953298276 hasConceptScore W2953298276C185592680 @default.
- W2953298276 hasConceptScore W2953298276C23265538 @default.
- W2953298276 hasConceptScore W2953298276C2781414619 @default.
- W2953298276 hasConceptScore W2953298276C55493867 @default.
- W2953298276 hasConceptScore W2953298276C59593255 @default.
- W2953298276 hasConceptScore W2953298276C62520636 @default.
- W2953298276 hasConceptScore W2953298276C71240020 @default.
- W2953298276 hasConceptScore W2953298276C75079739 @default.
- W2953298276 hasConceptScore W2953298276C8010536 @default.
- W2953298276 hasConceptScore W2953298276C86803240 @default.
- W2953298276 hasConceptScore W2953298276C91881484 @default.
- W2953298276 hasConceptScore W2953298276C935647 @default.
- W2953298276 hasConceptScore W2953298276C96305047 @default.
- W2953298276 hasLocation W29532982761 @default.
- W2953298276 hasOpenAccess W2953298276 @default.
- W2953298276 hasPrimaryLocation W29532982761 @default.
- W2953298276 hasRelatedWork W1461520417 @default.
- W2953298276 hasRelatedWork W1962144406 @default.
- W2953298276 hasRelatedWork W1978305202 @default.
- W2953298276 hasRelatedWork W1990223639 @default.
- W2953298276 hasRelatedWork W1993160633 @default.
- W2953298276 hasRelatedWork W2000094236 @default.
- W2953298276 hasRelatedWork W2002026976 @default.
- W2953298276 hasRelatedWork W2016271279 @default.
- W2953298276 hasRelatedWork W2035203385 @default.
- W2953298276 hasRelatedWork W2036132164 @default.
- W2953298276 hasRelatedWork W2051669882 @default.
- W2953298276 hasRelatedWork W2071266005 @default.
- W2953298276 hasRelatedWork W2072373904 @default.
- W2953298276 hasRelatedWork W2135339565 @default.
- W2953298276 hasRelatedWork W2153914131 @default.
- W2953298276 hasRelatedWork W2473350337 @default.
- W2953298276 hasRelatedWork W2497417600 @default.
- W2953298276 hasRelatedWork W3135245632 @default.
- W2953298276 hasRelatedWork W2051259976 @default.
- W2953298276 isParatext "false" @default.
- W2953298276 isRetracted "false" @default.
- W2953298276 magId "2953298276" @default.
- W2953298276 workType "article" @default.