Multiple Sequence Variants in STAC3 Affect Interactions with CaV1.1 and Excitation-Contraction Coupling-Reference-Cited by-同舟云学术

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Multiple Sequence Variants in STAC3 Affect Interactions with CaV1.1 and Excitation-Contraction Coupling

Published:2020-08 Issue:8 Volume:28 Page:922-932.e5
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Rufenach Britany,Christy Darren,Flucher Bernhard E.,Bui Jennifer M.,Gsponer Jörg,Campiglio Marta,Van Petegem Filip

Funder

Natural Sciences and Engineering Research Council of Canada

RYR-1 Foundation

Canadian Institutes of Health Research

Austrian Science Fund

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference47 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution;Adams;Acta Crystallogr. D Biol. Crystallogr.,2010

2. Molecular dynamics simulations at constant pressure and-or temperature;Andersen;J. Chem. Phys.,1980

3. Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle;Block;J. Cell Biol.,1988

4. Phosphorylation of an intrinsically disordered segment in Ets1 shifts conformational sampling toward binding-competent substates;Bui;Structure,2014

5. STAC proteins associate to the IQ domain of CaV1.2 and inhibit calcium-dependent inactivation;Campiglio;Proc. Natl. Acad. Sci. U S A,2018

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